SYMPOSIUM: PROTEIN AND FIBER DIGESTION,
PASSAGE AND UTILIZATION IN LACTATING COWS
Protein Supply from Undegraded Dietary Protein
ABSTRACT
A summary of in vivo estimates of the
amotint of dietary protein from in-
dividual feedstuffs that escapes micro-
bial degradation in the rumen is pre-
sented. Values range from approximately
20% for protein in barley, oats, wheat,
and alfalfa silage to 65 to 70% for protein
in fish meal and animal by-products. In
vitro or in situ methods for estimating
protein degradation can be used, but at
this stage of development, the meth-
odology is more useful in providing a
relative ranking of feedstuffs on the basis
of protein degradation than in providing
absolute estimates of protein degradation.
A number of factors influence protein
breakdown in the rumen, including
extent of crosslinking in the protein
(disulfide bonds), retention time in the
rumen, protein solubility, and processing
and storage effects on protein. It is
important to consider the amino acid
content of the undegraded dietary
protein, particularly lysine and methio-
nine, two amino acids likely to be limit-
ing for milk production. Strategies for
using protected proteins in dairy cattle
diets are discussed.
INTRODUCTION
Amino acids absorbed from the ruminant's
small intestine have their origin in rumen
microbes, undegraded dietary protein, and
endogenous protein. Microbial protein supplies
approximately two-thirds of the ruminant's
amino acids, and dietary protein accounts for
most of the remainder. Numerous factors can
influence this proportion by altering microbial
yield and protein degradation in the rumen.
Received August 30, 1985.
1986 J Dairy Sci 69:2734-2749
L A R R Y D. SATTER
US Dairy Forage Research Center
US Department of Agriculture,
Agricultural Research Service
University of Wisconsin Madison 53706
This review is an overview of protein degrada-
tion in the rumen and its significance for the
lactating cow.
E X T E N T OF P R O T E I N D E G R A D A T I O N
IN THE R U M E N
Information about protein degradation in
the mmen is required by the new protein
systems that have been proposed to replace
crude or digestible protein in feeding standards
(6, 60, 74). Table 1 contains estimates of the
percentage of crude protein in various feed-
stutts that escapes destruction in the reticu-
lorumen. All estimates were obtained with
sheep or cattle having abomasal or duodenal
cannulae. Estimates of the amount of protein
escaping degradation in the reticulorumen are
extremely variable and in vivo information is
limited or nonexistent for many feedstuffs.
Some of the variation among estimates of
protein degradation in vivo is due to the dif-
ficulty of measuring flow and obtaining re-
presentative samples of abomasal or duodenal
digesta. This is compounded by the problem of
distinguishing between microbial and dietary
protein. Differences among diets, residence
time in the rumen, and the feedstuff itself are
some reasons why the range in reported values
is so large in Table 1.
The last column in Table 1 is my estimate of
an average for undegraded protein based on in
vivo, in vitro, and in situ information. Numbers
are rounded to emphasize the lack of precision
in the estimates. These are relative numbers,
and the extent of protein degradation for a
feed will vary with the feeding situation. The
reliability of the estimates varies across the
feeds. The estimate for soybean meal is reason-
ably accurate, but less confidence can be placed
in most of the other estimates because rel-
atively few measurements have been made.
Generally speaking, in vivo estimates of protein
degradation for high protein feeds are more
accurate than for low protein feeds. The reason
2734
 SYMPOSIUM: PROTEIN AND FIBER DIGESTION 2735

TABLE 1. In vivo estimates of undegraded protein for c o m m o n feedstuffs when total dry matter intake is in
excess of two percent of body weight.

Measured
fraction of Adjusted References
Number of Range of undegraded fraction of for in
measure- measure- protein undegraded vivo
Feed ments ments (mean) 1 protein 2 experiments

Feedgrains
Barley 2 . 1 4 - .28 .21 .20 36,37
Oats 0 . . . . . . . 20
Wheat 0 . . . . . . . 20
Corn 3 . 5 8 - .73 .65 .50 1,79
Milo 8 . 2 0 - .69 .52 .50 23,55,69
Oil meals
Peanut 2 .22- .37 .30 .25 25, 42
Sunflower 2 .19- .28 .24 .25 42
Canola 1 . . . . 23 .25 59
Linseed 1 . . . . 44 .30 78
Soybean 13 .10-- .61 .27 .30 17, 25, 30, 32
40, 50, 59, 71
78, 79
Cottonseed (solvent) 6 . 2 4 - .61 .41 .35 17, 78, 79
Cottonseed (prepress) 2 . 3 5 - .38 .36 .40 17
Cottonseed (screw press) 2 . 4 3 - .57 .50 .45 17
By-product feeds
Corn gluten feed 2 .14-- .26 .20 .20 12
Brewers dried grains 5 . 2 7 - .66 .53 .50 40, 53, 61, 77
Corn gluten meal 3 .46-- .51 .55 .55 66, 78
Distillers dried grains 4 . 4 7 - .68 .56 .55 12, 61, 77
Blood meal 2 .54-- .82 .68 .65 32, 50
Meat and bone meal 2 . 4 9 - .70 .60 .65 32, 78
Fish meal 6 .69-1.00 .80 .70 9, 25, 39, 42
Meat meal 1 . . . . 76 .70 79
Forages
Alfalfa silage 1 . . . . 17 .20--. 30 56
Alfalfa silage with formic 1 . . . . 18 .20 63
acid
Alfalfa hay 6 . 0 9 - .41 .23 .25 2, 27, 36, 45
52, 56
Alfalfa silage with 1 . . . . 33 .30 63
formic acid and
formaldehyde
Bromegrass hay 2 .21-- .44 .32 .30 27, 37
Timothy hay 2 .28- .48 .38 .30 4
Corn silage 1 . . . . 27 .30 9
Coastal bermuda grass 1 . . . . 20 .30 2
Coastal bermuda grass 1 . . . . 40 .40 2
(dehydrated)
Alfalfa (dehydrated) 4 . 4 3 - .66 .56 .50 2, 32, 79
Other
Soybeans 0 .20
Cottonseed 0 .30

1Expressed as a fraction of total crude protein.

2The mean of the in vivo measurements has been adjusted to reflect in vitro and in situ information on
protein degradation. Also, values have been rounded.

Journal o f Dairy Science Vol. 69, No. 10, 1986

2736 SATTER
for this is that incremental additions of a high
protein feed to the diet allows estimation of
undegraded protein by regression analyses (43,
67). With low protein feeds, the amount of
undegraded protein in the experimental feed
must be calculated as the difference between
flow of total protein and microbial protein at
the abomasum or duodenum. This makes the
estimate very dependent upon accurate mea-
surement of microbial protein, which is an
unlikely event. Unfortunately, most values in
Table 1 were calculated by difference.
Corn, oats, barley, alfalfa, corn silage,
brewers grains, distillers grains, soybean meal,
cottonseed meal, and cottonseeds provide the
majority of protein in dairy cattle diets in
North America, yet the accuracy of estimates
for protein degradation with most of these
feeds is poor. Most in vivo measurements of
protein degradation have been with by-product
feeds and relatively few with the feed grains
and forages, which provide the bulk of protein
in dairy cattle diets.
As pointed out earlier, the values in Table 1
are useful to rank feeds on the basis of sus-
ceptibility to protein degradation, but they
may not be appropriate for each feeding
situation. Residence time in the rumen and rate
of proteolysis and deamination varies with the
feeding situation, thus affecting protein de-
gradation. Ideally, information on residence
time and rate of protein degradation would
enable prediction of protein degradation under
a variety of conditions. Another problem with
the values in Table 1 is that variation in protein
degradation within a feed can be large, par-
ticularly with by-product feeds. For example,
differences in processing or drying conditions
can affect protein degradation, and variation
from one supplier to another can be significant.
Protein degradation has been described as a
function of time in many in vitro and in situ
experiments (10, 29, 42, 47, 51). Most of these
data fit a general model with three protein
pools: pool A, nonprotein nitrogen (NPN) or
protein that is degraded very rapidly; pool B,
protein degraded at a rate similar to the frac-
tional rate of digesta passage from the re-
ticulorumen (approximately .02 to .2 h - l ) ;
and pool C, bound or unavailable protein
degraded very slowly or not at all.
Ideally, each pool has a degradation rate that
is assumed fractional, that is, a constant pro-
Journal of Dairy Science Vol. 69, No. 10, 1986
portion of the remaining protein is degraded
per unit of time. The fractional degradation
rates per hour are: kdA, = fractional degrada-
tion rate for A and greater than 10 times the
rate of digesta passage from the reticulo-rumen;
kdB , = fractional degradation rate for B and
may be between 10 times and .10 the rate of
passage; and kdc, = fractional degradation rate
for C and less than one-tenth the rate of passage.
In practice, kdA might be considered suf-
ficiently large relative to rate of digesta passage
that essentially all of pool A protein is degraded.
The opposite is true for kdC, where it is so
small relative to rate of passage that pool C
protein is considered totally undegraded. Only
degradation of pool B protein will be affected
by the relative rate of passage, which for pool B
is kpB. Therefore, the fraction of total protein
that is degraded (D) is:
D = A + kdBB/(kdB + kpB)
The fraction of total protein that is passed
out of the reticulorumen (P) is:
P = kpBB/(kdB + kpB) + C
The obvious advantage for using fractional
rate constants to calculate the amount of
undegraded protein is that information about
residence time and rate of proteolysis can be
applied to the specific feeding situation. This
has the potential of being more accurate than
an average value (Table 1), which may have
been determined under much different feeding
conditions. The problem with this approach,
however, is that very little information about
kpB and kdB exists for our common feeds.
Furthermore, techniques for accurately mea-
suring kpB and kdB are lacking, as are pro-
cedures for quantitating Fractions A, B, and C.
Techniques exist that may provide first
approximations of kpB , kdB , A, B, and C. Rare
earth elements (65) or chromium mordants
(13) have been used as markers of dietary
protein passage through the reticulorumen and
can provide reasonable estimates of kpB. It is
more difficult to measure kdB. Feeds contain
several types of protein that are in the B
fraction, and presumably each protein has its
own kdB. Existing procedures do not sort out
the individual rate constants but do yield an
average rate. The nylon bag technique described
 SYMPOSIUM: PROTEIN AND FIBER DIGESTION 2737

by Orskov et al. (47), for example, has been
used to estimate kdB and pools A and B as well.
The amount of protein that leaves the bag upon
washing or following 1 h incubation in the
rumen and subsequent washing is considered
equal to pool A. Pool A, as measured by this
technique, consists of soluble proteins and
protein residing in very small particles that are
removed when the bag is washed. A troubling
aspect of this is that Mahadevan et al. (34) have
demonstrated that the protease in Bacteroides
arnylopbilus hydrolyzed some insoluble pro-
teins more rapidly than soluble proteins. It is
erroneous to assume that all soluble proteins
are degraded in the rumen.
To estimate pool B with the in situ bag
technique the rapidly disappearing fraction of
protein (pool A) is subtracted from the amount
of protein leaving the bag after an extended
incubation of 48 to 72 h. Pool C might be
considered as the portion of protein remaining
in the bag after 48 to 72 h. Figure 1 sum-
marizes the foregoing discussion of how the in
situ bag technique might be used to calculate
kdB and pools A, B, and C.
The in situ bag technique has many short-
comings and is subject to a number of variables
(44, 47, 76). Pore size of the bag material has
large influence on the results. Pores of ap-
proximately 50 /am give results that appear
reasonable. There is no question that the in situ
bag technique is an empirical approach and has
many unsettling aspects. It may serve a pur-
pose, however, until more suitable techniques
emerge.
Other in vitro techniques to estimate diges-
tion rates for protein have been proposed. In
vitro measurements using either rumen in-
oculum (10, 33) or commercially available
proteases (7, 29, 54) have been reported. The

100 ~--THIS PART OF CURVE DESCRIBED BY '-~ "lr"

FRACTION

F ION

-- G

~ / A a FRACTION A (PROTEIN RAPIDLY DEGRADED)

q0, ~" B z FRACTION B (PROTEIN POTENTIALLy DEGRADED
/ = _ AT A MODERATE RATE)
C FRACTION C ~ROTEIN)
(UNAVAILABLE
- FRACT|ONAL RATE CONSTANT FOR
20. I "KdB DEGRADATIONOF PROTEIN IN FRACTION B
J FRACTION
J~ T = INCUBATION TIME A

0 ~
0 2q g8 72
INCUBATION TIRE
Figure 1. Disappearance of protein from the in situ bag and its use for designating fractions A, B, and C in
feed proteins.

Journal of Dairy Science Vol. 69, No. 10, 1986

2738
study by Krishnamoorthy et al. (29) utilized
information on rate of passage as well as rate of
digestion to predict protein degradation and
concluded that protease from Streptomyces
griseus was superior to the in situ bag technique
for estimating protein breakdown. Protein
solubilization by S. griseus protease, when
plotted with time (29), was used to identify
protein pools A, B, and C. In this study, pool B
was subdivided into three fractions, B l, B2, and
B3. Protein unavailable to the S. griseus pro-
tease after 48 h exposure was considered as the
C pool, and the size of this pool C approached
hut did not equal the amount of acid detergent
insoluble nitrogen (ADIN) (14).
A major limitation with the in vitro rumen
or protease systems is that the rate constant for
protein degradation determined with a lab-
oratory procedure may differ considerably
from that determined in vivo. Incubation pH,
numbers of organisms, and amount of protease
are just a few of the variables that can greatly
influence the rate constant determined in vitro.
Relative values for fractional degradation rates
among protein sources may be obtainable, but
accurate absolute values are required, and with
current procedures this is unlikely. The in vitro
or protease procedures could be very useful,
however, in ranking similar feeds or evaluating
the effect of chemical or heat treatment on
protein degradation within a feed.
Rumen fermentation is a dynamic process,
and many significant events in the process can
be simplified to involve only two or three pools
whose turnover can be described by first order
kinetics. Researchers must strive for quanti-
tative mathematical description of the digestive
process. This modeling exercise can enhance
our inquiry and eventual understanding of the
process. However, until more is known about
the dynamics of protein degradation and how
to quantitate it, practical ration formulation
utilizing information on protein degradation
will have to be based on the type of informa-
tion in Table 1.
FACTORS INFLUENCING PROTEIN
D E G R A D A T I O N IN THE F O R E S T O M A C H
The extent of protein degradation in the
rumen is dependent upon microbial activity and
access to the protein. Characteristics of the
protein itself and the feed particle in which the
protein residues are also influential.
Journal of Dairy Science Vol. 69, No. 10, 1986
SATTER
Tertiary Structure of the Protein
Access to protein by proteolytic enzymes is
influenced by the three-dimensional structure
of the protein molecule. Proteins with extensive
crosslinking, such as disulfide bonds, are less
accessible to proteolytic enzymes and are rel-
atively resistant to degradation (46). Proteins in
hair and feathers are examples of highly cross-
linked proteins. Treatment of protein with
formaldehyde causes methylene crosslinking,
thus reducing rate of proteolysis (11). A further
example of the influence of tertiary structure is
provided by ovalbumin. Ovalbumin is a soluble
but cyclic protein having no terminal amino or
carboxyl groups. The cyclic feature greatly
reduces the rate of proteolysis (35). These and
other features of protein structure influence
vulnerability of protein to hydrolysis in the
rumen.
Retention Time in the Rumen
Extent of protein degradation is influenced
by the residence time of protein in the rumen.
The significance of residence time depends
upon the fractional degradation rate of protein.
This is illustrated in Table 2 where protein
degradation values were calculated from the
relationship discussed earlier: protein degrada-
tion (D): A + kdB B/(kdB + kpB). Many
protein supplements and most feeds have a
ruminal passage rate (kpB) within the range of
.03 to .07 h - 1 (13, 20, 67). Pools A and C
were set at .2 and .1 for the calculations for
Table 2, thus making pool B equal .7. Allowing
kdB to range from .03 to .48, rate of passage
effect is greatest when rate of protein degrada-
tion is low (Table 2). If the fractional degrada-
tion rate of protein is .12, increasing rate of
passage from .03 to .07 causes protein de-
gradation to decrease from .76 to .64. This is a
rather modest change in degradation as a result
of a large change in rumen retention time.
High producing ruminants consuming large
quantities of feed are likely to have a smaller
fraction of dietary protein degraded in the
rumen than animals consuming low or moderate
amounts. The amount of undegraded dietary
protein as a percent of total dietary protein was
29 and 45% for cows consuming 8.2 or 12.9 kg
of dry matter daily (68). Effect of intake on
retention time of feed particles, however, is
sometimes quite small (20, 73), and the impact
 SYMPOSIUM: PROTEIN AND FIBER DIGESTION
TABLE 2. Effect of fractional rate of protein degradation and rate of passage on protein degradation (D).
Fractional rate of Fractionalrate of protein degradation/h(KdB)
passage/h (KpB) 103 .06
.03 .55 .67
.04 .50 .62
.05 .46 .58
.06 .43 .55
.07 .41 .52
on protein degradation may often be minor
(42) or without effect (38).
Increasing the dilution rate of rumen fluid
can increase flow of protein from the rumen of
sheep (19) and steers (8, 57). Part of this
increase is probably due to a net increase in
bacterial protein (18, 19) and part due to an
increase in the proportion of undegraded
dietary protein (21). Rumen fluid dilution rates
have been increased by feeding or by ruminal
infusion of artificial saliva, sodium bicarbonate,
or sodium chloride.
Environmental temperatures influence the
residence time of feed in the rumen. Kennedy
et al. (26) demonstrated that sheep in a cold
environment had increased rate of digesta
passage. This increased the amount of microbial
crude protein and the amount of undegraded
dietary protein. In a subsequent study, Kennedy
et al. (27) found that the percentage of un-
degraded dietary protein increased from 20 to
24% for alfalfa hay and from 40 to 49% for
bromegrass hay when sheep were exposed to
cold temperatures. No effect of temperature on
extent of protein degradation of a barley-canola
seed meal diet was observed, however.
Quantity of feed intake may have some
effect on protein degradation aside from
influencing residence time. Lower rumen pH,
which usually accompanies increased feed
intake, may reduce bacterial and proteolytic
activity. Rumen pH is normally between 5.5
and 7.0, and proteins with an isoelectric point
in this range would have altered solubility
and possibly altered protein degradability. Also,
fiber may limit microbial access to plant
protein, and reduced fiber digestion at a lower
pH might be involved as well (13).
2739
.12 .24 148
(D)
.76 .82 .86
.73 .80 .85
.69 .78 .83
.67 .76 .82
.64 .74 .81
Protein Solubility
Soluble proteins tend to be more rapidly or
completely degraded than insoluble proteins
(22). Access to protein by proteases is greater if
the protein is in solution. It seems likely,
however, that some feed protein can by hy-
drolyzed directly from the solid phase without
an intervening soluble phase, similar to the
digestion of cellulose.
Soluble proteins differ greatly in the rate at
which they are hydrolyzed. Nugent and Mangan
(46) studied the degradation of casein, fraction
I leaf protein, and bovine serum albumin in
vitro using sheep rumen fluid. All three proteins
were soluble in buffer but differed greatly in
the rate at which they were hydrolyzed (casein
> fraction I leaf protein > bovine serum
albumin). This, and the work of Mahadevan et
al. (34), suggests that differences in the rates of
microbial hydrolysis of some proteins are
caused by structural and not solubility dif-
ferences.
Protein solubility as a measure of protein
degradation can lead to serious error when
applied across a variety of feeds. However,
Beever et al. (5) found high correlation (r 2 =
.96) between soluble N in perennial ryegrass,
determined as the N soluble after incubation
with .01 percent pepsin in .1 N HC1 for 16 h,
and the quantity of total nitrogen entering the
small intestine. Solubility and, in this case, the
degradation of ryegrass protein were altered by
drying at different temperatures and by form-
aldehyde treatment. It is reasonable to expect
protein solubility to predict differences in
protein degradation more accurately when
applied to a group of similar feeds than when
used across a diverse group of feeds differing in
Journal of Dairy Science Vol. 69, No. 10, 1986
2740 SATTER

physical and chemical properties. In conclusion,
protein solubility can be a simple and useful
technique to monitor treatment effects on a
given protein source, but it cannot be relied
upon to predict degradation across a diverse
group of feeds.
Feed Processingand Storage
Some feeds are exposed to heat during
processing or storage. By-product feeds are
often dried for marketing, and ensiled feeds
may experience elevated temperatures for a
sustained time. Feed processing methods such
as pelleting, extrusion, and steam rolling and
flaking may generate enough heat to alter
protein. A limited amount of heat-processed or
chemically treated protein is presently being
marketed for ruminants in the United States.
Figure 2 illustrates the relationship amoung
protein degradation, protein availability, and
heat input. As heat input is increased, amount
of undegraded protein increases. Amount of
unavailable protein also increases, but initially
the quantity of unavailable protein formed is
less than the amount of protein protected from
degradation. The maximum amount of protein
available for digestion in the small intestine will
most likely occur when there is a modest
amount of heat damage to the protein, The
temperature × time product of the abscissa
(Figure 2) is not necessarily a linear function.
There may be a temperature threshold above
which protein needs to be heated before there
is significant protection.
It is important to know the exact shape of
the curves in Figure 2 for each of the heat-
treated feeds to obtain maximum benefit from

100
UNDEGRADED
PROTEIN

80
DEGRADED UNAVAILABLE
PROTEIN PROTEIN

pMAXIHUH SUPPLY OF
I.-
Z PROTEIN AVAILABLE FOR
t~
U
rv, 40 DIGESTIqN IN THE
U,I
SMALL INTESTINE

20

HEAT INPUT (TEHPERATURE X TIME)

Figure 2. Effect of heat input on protein utilization. Modified from Van Soest (72).

of
Journal Dairy Science Vol. 69, No. 10, 1986
 SYMPOSIUM: PROTEIN AND FIBER DIGESTION
the heating process. F o r whole cottonseed, a
temperature of 160°C for 20 min provides
about the same amount of protection as 140°C
for 60 min. If heat exposure is limited to less
than 12 min, temperatures in excess of 180°C
will be required (49). Ensiled forages may
undergo effective heat treatment at tempera-
tures as low as 40 to 45°C, provided the tem-
perature is sustained for 3 mo or more (41).
Moisture, quantity of soluble carbohydrate
present, and maximum temperature are some of
the many factors that determine effectiveness
of heat in protecting protein from degradation
in the rumen (16).
An increased awareness of "heat damage" in
forages has come through widespread forage
analyses. The ADIN fraction is considered to
represent unavailable protein (15, 70), and
some users of forage analyses information have
been deducting the protein equivalent in the
ADIN fraction from the total protein content,
reasoning that it is unavailable and therefore
should not be counted. This is not appropriate
for two reasons. First, all forages have some
nitrogen in the ADIN fraction, and protein
feeding recommendations have been developed
with this in mind. Second, a modest amount of
"heat damage" to forage m a y be beneficial.
This can be visualized from Figure 2 and is
supported b y the experimental results of
Merchen and Satter (41) in Table 3. Lactating
cows fed diets containing 65% alfalfa forage
and 35% grain mix actuall~¢ absorbed more
TABLE 3. Nitrogen utilization by lactating cows fed diets containing alfalfa having four different moisture
contents (41).
Silage
Measurement (29% DM) ~
ADINz Content of forage, % of total nitrogen 7.9
Nitrogen intake, g/d 476 bc
Apparent nitrogen digestibility, % 72.3 a
Dietary amino acid intake, g/d 1570 h
Amino acids at duodenum, g/d 1526 b
Amino acids absorbed from small intestine, g/d 1075
Amino acid availability in small intestine, % 70.6
a'b'CMeans within a row having a different superscript differ (P<.05).
1DM = Dry matter.
~ADIN = Acid detergent insoluble nitrogen.
2741
amino acids from the intestine when the diet
contained alfalfa with 12.9% ADIN than when
a more normal a m o u n t o f 8 to 10% was present
in the alfalfa. This experiment is not inter-
preted to mean that some "heat damage" is
desired, for heat damage simply is too hard to
control, b u t forage with modest heat damage
should not be penalized. Whereas some users of
ADIN values may deduct all nitrogen contained
in the ADIN fraction from the potentially
useful crude protein, a larger number deduct
only t h a t - n i t r o g e n in the ADIN fraction that
exceeds approximately 10% of total nitrogen in
the forage. There is need to identify the amount
of "heat damage" that can be accepted before
allowing some depreciation in protein value.
Formaldehyde has been used to protect
protein from breakdown in the rumen. Feeding
trials with formaldehyde-treated casein ap-
peared very promising (11), and extensive
experiments with formaldehyde treatment of
forage have been conducted. Research with
aldehydes has emphasized the extent of pro-
tection achievable, and relatively little in-
formation on protein availability has emerged
(3, 63, 75). Although treatment of commercial
protein supplements with formaldehyde has
been disappointing, a combination of formic
acid-formaldehyde can be used to assist pre-
servation of direct-cut forages (63, 75). Form-
aldehyde is used to some extent in Europe for
this purpose, but the practice is not permissible
in North America.
Source of alfalfa
Silage Silage
(40% DM) (66% DM) Hay
7.5 12.9 10.4
542 a 501 ab 432 c
72.4 a 67.6 b 71.0 ab
2187 a 2257 a 1753 b
1815 ab 2041 a 1517 b
1284 1517 1090
70.3 74.3 72.5
Journal of Dairy Science Vol. 69, No. 10, 1986
2742
There is potential benefit from protecting
feed protein from excessive destruction and loss
in the rumen. One of the major advantages of
feeding protected protein would be greater
opportunity for utilization of nonprotein
nitrogen (NPN) for microbial synthesis in the
rumen and the economy inherent with NPN
use. A balance is needed, however, in the
amount of undegraded dietary protein and the
amount of dietary nitrogen made available for
microbial synthesis of protein. Much remains to
be learned about practical methods for altering
protein degradation in the rumen. More com-
plete summaries of nitrogen utilization by
ruminants are available (24, 31, 48).
I M P O R T A N C E OF P R O T E I N Q U A L I T Y
It is important to know how protein sources
differ in their susceptibility to breakdown in
the rumen. It is equally important to know
something about protein quality, including
amino acid composition and availability of the
undegraded protein.
Lysine and methionine appear to be the first
limiting amino acids for lactating cows con-
suming a diet consisting primarily of corn, corn
silage, and limited amounts of alfzlfa-grass hay
(62). Lysine infusion resulted in 16% of the
total response in yield of milk protein that was
obtained with infusion of either the 10 essential
amino acids or sodium caseinate, while infusion
of lysine and methionine together accounted
for 43% of the total response. This suggests
that lysine and methionine are first and second
limiting, or colimiting, for secretion of milk
protein with diets high in corn and corn silage.
TABLE 4. Expected supply of lysine and methionine to the intestine when soybean meal and distillers dried
grains are fed.
Amino acid Source
Lysine Soybean meal
Distillers grains
Methionine Soybean meal
Distillers grains
Journal of Dairy Science Vol. 69, No. 10, 1986
SATTER
Table 4 illustrates how soybean meal and
distillers dried grains compare in their ability to
supply lysine and methionine to the intestine
for absorption. Soybean meal is an excellent
source of lysine, containing about 68 g lysine/
kg of protein. If 30% of the protein in soybean
meal escapes degradation in the rumen, then
20.5 g of lysine/kg of soybean protein fed
would escape to the intestine. Distillers grains,
notably low in lysine but containing a relatively
resistant protein, would be expected to supply
16.7 g in this example. Despite the much higher
content of undegraded protein in distillers
grains, it actually supplies less lysine to the
intestine than soybean meal. With methionine
the opposite is true. The protein in distillers
grains has a relatively high methionine content,
and this combined with less protein degradation
makes distillers grains an excellent source of
methionine relative to soybean meal.
It is clear that both amino acid content and
degradability of a feed protein must be con-
sidered in determining value of a protein in
ruminant diets. Stehr (64) explored this point
in a study involving 60 multiparous Holstein
cows in early lactation. Cows were divided into
four groups of 15 cows each to compare four
protein sources: conventional soybean meal
(SBM), extruded mixture of soybeans and
soybean meal (ES), a combination of distillers
dried grains with solubles and corn gluten meal
(DC), and a mixture of equal parts of sup-
plements ES and DC (ES/DC). Complete
mixed diets were fed consisting of corn silage,
coarse ground corn with added mineral and
vitamin supplement, and one of the four
protein sources. Each diet averaged 14.5 to
Amino acid Fraction
in 1 kg of protein Amino acid
protein escaping escaping
(g) (g)
68.2 .30 20.5
30. 3 .55 16.7
11.4 .30 3.4
16.2 .55 8.9
 SYMPOSIUM: PROTEIN AND FIBER DIGESTION 2743

15.0% crude protein, dry matter basis. Cows
were fed a standardization diet for the first 10
d following calving and then were randomly
assigned to one of the four test diets for d 11 to
40 of lactation. Milk production from d 20 to
40 of lactation were adjusted by covariant
analysis with milk production measured during
d 4 to 10 of the standardization period serving
as the covariant.
The experimental results are shown in Table
5. Pretreatment milk production was similar for
the four groups. Treatment milk production
was highest for the ES supplement, followed by
the SBM, ES/DC, and DC treatments. Based on
the amount of undegraded protein in each diet,
treatments ES, DC, and ES/DC should have
supported higher milk production than the
SBM treatment. Treatment DC supported the
lowest milk production, and treatment ES/DC
was intermediate between ES and DC, as it
should be since it is a mixture of ES and DC. If
lysine is the first limiting amino acid for milk
production with the basal diet, then treatment
ES would be expected to support the highest
milk production and treatment DC the least.
The high content of undegraded protein in DC
appeared not to overcome the low lysine
content. This experiment suggests diets con-
taining primarily corn and corn silage should
not be supplemented with corn-based protein
supplements.
STRATEGIES FOR USING PROTECTED
PROTEINS IN D A I R Y DIETS
There are at least three strategies that may
be used in feeding relatively resistant proteins
to lactating dairy cows. The first involves a
simple substitution of the conventional protein
supplement with an equal amount of protein
from a relatively resistant protein source. This
is in anticipation of higher milk production.
This strategy is illustrated in Figure 3.
Contained in Figure 3 is a milk production
response curve developed from 17 lactation
studies involving 625 cows (58). The cows used
in this summary were in early lactation and had
potential milk production of approximately
7000 kg. Corn silage was the primary forage,
and soybean meal was the source of supple-
mental protein. Change in milk production per
unit supplemental protein was greatest with low
protein and diminished rapidly as the amount
of protein in the diet increased. Point A in
Figure 3 corresponds to the amount of milk
expected with the unsupplemented " h o m e
grown" feeds, which in this example, contain
12% protein. If a conventional protein sup-
plement, such as soybean meal, is used to raise
the dietary protein content from 12 to 15%,
milk production designated by point B is
expected that is equal to an increase of 3.2 kg
milk/cow/d.

TABLE 5. Effect of source of supplemental protein on milk production, milk composition, and dry matter
intake.

Diet I
Measurement SBM ES DC ES/DC SE

Pretreatment milk, kg/d 27.2 27.1 26,9 27.8 1.44

Treatment
Milk, kg/d 37.5 a 38.5 a 31.8 b 35.2 ab 1.64
Milk fat, % 3.14 3.19 3.45 3.08 .16
Protein, % 3.14 a 2.93 b 2.72 c 2.98 ab .05
Dry matter intake, kg/d 22.5 a 21.3 ab 19.9 b 22.4 a 1.00

a'b'CMeans within a row having different superscripts differ (P<.05).

1SBM = Soybean meal, ES = extruded mixture of soybeans and soybean meal, DC = distillers dry grains
with solubles and corn gluten meal, ES/DC = equal parts of ES and DC.

Journal of Dairy Science Vol. 69, No. 10, 1986

2744
32 "
28 "
o
" 24 -.
FEEDS HEM-TREATED SUPPLEI,IEN T . . . . .
11 12 13
Z DIETARY PROTEIN
Figure 3. Illustration of strategy one for utilizing heat-processed protein supplements (see text for details).
The example used to illustrate the first
strategy, therefore, involves substitution of a
protected source of soybean meal for the
conventional soybean meal. In this example, we
assume that heat processing of soybean meal
has increased the amount of undegraded
protein from 30 to 45%. It is further assumed
that the "home grown" or basal portion of the
diet supplies adequate nitrogen for the rumen
microbes. Thus, only the undegraded protein in
the supplemental soybean meal will be of value
as a protein source. The same quantity of
heated soybean meal is used to replace the
conventional soybean meal, so crude protein
content remains at 15%. However, the heated
soybean meal supplies half again as much
undegraded, or by-pass, protein. Therefore, in
this example, that means the diet with heat-
treated soybean meal containing 15% crude
protein is equivalent to a conventional soybean
Journal of Dairy Science Vol. 69, No. 10, 1986
SATTER
~ . 9 KG
3.2 KG
14 15 16 17 18
meal diet containing 16.5% crude protein
(point C). The amount of additional milk
expected from the substitution of heated
soybean meal for conventional soybean meal in
this example is small (.9 kg) because the milk
production response curve is flattening out.
The obvious question the dairy farmer must ask
when employing this strategy is whether the
anticipated increase in milk production from
feeding a protected protein will pay for the
additional cost of protein protection. This
strategy has limitations because of the shape of
the milk production response curve and may in
part explain why milk production results have
often been disappointing with use of protected
proteins.
Another strategy for using protected protein
is to replace the conventional protein sup-
plement with a smaller quantity of the rel-
atively resistant protein. An example of this is
 SYMPOSIUM: PROTEIN AND FIBER DIGESTION
illustrated in Figure 4. The same amount of
protein would need to be supplied to the
intestine for absorption; however, less resistant
protein supplement would be needed. Milk
production should not be affected, but hope-
fully cost of protein supplementation could be
lowered, because less total protein would be
used. This strategy is limited to diets moderate
to high in protein. Otherwise, a shortage
of nitrogen for the rumen microbes could
develop.
A third potential strategy involves com-
bining a low cost nonprotein nitrogen source
with a resistant protein supplement and an
energy source (shelled corn) to give a low cost
mixture that may substitute for the conven-
tional protein supplement. Again, change in
32
II
28
24
- CONVENTIONAL
FEED SUPPLEMENT
i
II II
w •
12 13
Figure 4. Illustration of strategy two for utilizing heat-processed protein supplements (see text for details).
2745
milk production would not be expected but
hopefully cost of supplementation would be
reduced. Klopfenstein et al. (28), working with
growing beef cattle, suggested different com-
binations of urea, resistant protein sources, and
corn that are approximately equal to soy-
bean meal in terms of energy, ammonia supply
to rumen microbes, and protein supply to the
small intestine. These combinations are in Table
6. These different mixtures are considered
approximately equal for growing beef animals,
and they will not necessarily be equivalent for
lactating dairy cattle. Differences in price
among these formulations can be large, thus
affording opportunity for savings.
The objective of this strategy, as in the
second strategy discussed, is to lower cost of
SUPPLEMENTII
m Q IP ~IP
I•
•
lg 15 16 17 18
DIETARY PROTEIN
Journal of Dairy Science Vol. 69, No. 10, 1986
 2746 SATTER
TABLE 6. Mixtures of relatively resistant protein sources, shelled corn and urea that are approximately equi-
valent to soybean meal for growing cattle (28).
Protein
source
Soybean meal 2000
Corn gluten meal 643
Brewers grains 1619
Distillers grains 1853
Distillers grains with solubles 2346
Dehydrated alfalfa 2788
Blood meal, ring dried 365
Blood meal, conventional 458
Meat meal 885
protein s u p p l e m e n t a t i o n , in this i n s t a n c e
b e c a u s e o f t h e low cost o f n o n p r o t e i n n i t r o g e n .
I m p r o v i n g a n i m a l p e r f o r m a n c e is n o t a n ob-
j e c t i v e in t h i s strategy. T h i s s t r a t e g y is m o s t
a p p l i c a b l e w i t h m o d e r a t e t o low p r o t e i n diets.
With high p r o t e i n diets t h e r e w o u l d be n o n e e d
t o i n c l u d e u r e a in t h e b l e n d b e c a u s e of t h e
e x i s t i n g surplus o f a m m o n i a in t h e t u r e e n .
SUMMARY
I n f o r m a t i o n is available regarding e x t e n t o f
p r o t e i n d e g r a d a t i o n f o r s o m e m a j o r feeds, b u t
i n f o r m a t i o n is lacking for m a n y m i n o r feeds.
C a u t i o n m u s t b e used w h e n f o r m u l a t i n g diets
o n t h e basis o f p r o t e i n d e g r a d a t i o n . P r o t e i n
sources differ grately in t h e i r s u s c e p t i b i l i t y t o
b r e a k d o w n in t h e r u m e n , b u t b e i n g r e s i s t a n t t o
m i c r o b i a l d e g r a d a t i o n does n o t necessarily
m e a n t h e y will s u p p o r t high m i l k p r o d u c t i o n .
A d e q u a t e a t t e n t i o n m u s t b e given to a m i n o
acid c o n t e n t of t h e p r o t e i n a n d also t o p r o t e i n
s t a t u s o f t h e animal.
O n e o f several strategies m a y b e u s e d f o r
i n c o r p o r a t i n g r e s i s t a n t p r o t e i n s i n t o t h e dairy
diet. T h e s t r a t e g y of c h o i c e will d e p e n d u p o n
t h e diet, p h y s i o l o g i c a l s t a t e o f t h e animal, a n d
cost o f feed ingredients. P e r h a p s t h e m o s t
p r o m i s i n g s t r a t e g y involves c o m b i n i n g a re-
sistant protein source with nonprotein nitrogen,
t h u s t a k i n g a d v a n t a g e o f t h e savings f r o m use o f
nonprotein nitrogen.
REFERENCES
1 Aguirre, E. O., A. L. Goetsch, and F. N. Owens.
1984. Fermented corn grain-site and extent of
Journal of Dairy Science Voi. 69, No. 10, 1986
Shelled
corn Urea
(kg)
1218 139
229 152
12 135
... 87
152
'1473 162
1405 137
984 131
nutrient digestion in steers. Oklahoma Agric. Exp.
Res. Rep. Misc. Publ. 116.
2 Amos, H. E., W. R. Windham, and J. J. Evans.
1984. Nitrogen metabolism of steers fed suncured
hay and drum dehydrated alfalfa and coastal
bermuda grass. J. Anita. Sci. 58:987.
3 Ashes, J. R., J. L. Mangan and G. S. Sidhu. 1984.
Nutritional availability of amino acids from protein
cross-linked to protect against degradation in the
rumen. Br. J. Nutr. 52:239.
4 Beever, D. E., D. F. Osbourn, S. B. Cammell, and
R. A. Terry. 1981. The effect of grinding and
pelleting on the digestion of Italian ryegrass and
timothy by sheep. Br. J. Nutr. 46: 357.
5 Beever, D. E., D. J. Thomson, and S. B. Cammell.
1976. The digestion of frozen and dried grass. J.
Agric. Sci. (Camb) 86:443.
6 Burroughs, W., D. K. Nelson, and D. R. Mertens.
1975. Protein physiology and its application in the
lactating cow: The metabolizable protein feeding
standard. J. Anim. Sci. 41:933.
7 Chamberlain, D. G., and P. C. Thomas. 1979.
Prospective laboratory methods for estimating the
susceptibility of feed proteins to microbial break-
down in the tureen. Proc. Nutr. Soc. 38:138A.
8 Cole, N. A., R. R. Johnson, F. N. Owens, and J. R.
Males. 1976. Influence of roughage level and corn
processing method on microbial protein synthesis
by steers. J. Anita. Sci. 43:497.
9 Cottrill, B. R., D. E. Beever, A. R. Austin, and D.
F. Osbourn. 1982. The effect of protein and
nonprotein nitrogen supplements to maize silage
on total amino acid supply in young cattle. Br. J.
Nutr. 48: 527.
10 Craig, W. M., B. J. Hong, G. A. Broderick, and R. J.
Bula. 1984. In vitro inoculum enriched with
particle-associated microorganisms for determining
rates of fiber digestion and protein degradation. J.
Dairy Sci. 67:2902.
11 Ferguson, K. A., J. A. Hemsley, and P. J. Reis.
1967. Nutrition and wool growth. The effect of
protecting dietary protein from microbial degrada-
 SYMPOSIUM: PROTEIN AND FIBER DIGESTION
tion. Aust. J. Sci. 30:215.
12 Firkins, J. L., L. L. Berger, G. C. Fahey, Jr., and N.
R. Merchen. 1984. Ruminal nitrogen degradability
and escape of wet and dry distillers grains and wet
and dry corn gluten feeds. J. Dairy Sci. 67:1936.
13 Garter, G., E. R. Orskov, and R. Smart. 1979. The
effect of roughage or concentrate feeding and
retention time on total degradation of protein in
the rumen. J. Agric. Sci. (Camb) 93:651.
14 Goering, H. K., C. H. Gordon, R. W. Hemken, D.
R. Waldo, P. J. Van Soest, and L. W. Smith. 1972.
Analytical estimates of nitrogen digestibility in
heat-damaged forages. J. Dairy Sci. 55:1275.
15 Goering, H. K., and P. J. Van Soest. 1970. Forage
fiber analysis (apparatus, reagents, procedures and
some applications). Agric. Handbook No. 379.
Agri. Res. Serv., US Dep. Agric.
16 Goering, H. K., and D. R. Waldo. 1978. The effects
of dehydration on protein utilization in ruminants.
Proc. 2rid Int. Green Chop Drying Congr., Univ.
Saskatchewan, Saskatoon, Can.
17 Goetsch, A. L., and F. N. Owens. 1985. The effects
of commercial processing m e t h o d of cottonseed
meal on site and extent o f digestion in cattle. J.
Anita. Sci. 60:803.
18 Harrison, D. G., and A. B. McAllan. 1980. Factors
affecting microbial growth yields in the reticulo-
rumen. Page 205 in Digestive physiology and
metabolism in ruminants. Y. Ruckebusch and P.
Thivend, ed. MTP Press, Lancaster, Engl.
19 Harrison, D. G., D. E. Beever, D. J. Thompson, and
D. F. Osbourn. 1975. Manipulation of tureen
fermentation in sheep by increasing the rate of
flow o f water from the rumen. J. Agric. Sci.
(Camb.) 85:93.
20 Hartnell, G. F., and L. D. Satter. 1979. Determina-
tion of rumen fill, retention time and ruminal
turnover rates o f ingesta at different stages of
lactation in dairy cows. J. Anita. Sci. 48: 381.
21 Hemsley, J. A. 1975. Effect of high intake of
sodium chloride on the utilization of a protein
concentrate by sheep. Aust. J. Agric. Res. 26: 709.
22 Henderickx, H., and J. Martin. 1963. In vitro study
of the nitrogen metabolism in the rumen. C. R.
Rech. Inst. Rech. Sci. Ind. Agric. Bruxelles 31:7.
23 Hibberd, C. A. 1982. Varietal, environmental and
processing effects on the nutritive characteristics of
sorghum grain. Ph.D. thesis, Oklahoma State Univ.,
Stillwater.
24 Huber, J. T., and L. Kung, Jr. 1981. Protein and
nonprotein nitrogen utilization in dairy cattle. J.
Dairy Sci. 64:1170.
25 Hume, I. D. 1974. The proportion of dietary
protein escaping degradation in the rumen of sheep
fed on various protein concentrates. Aust. J. Agric.
Res. 25:155.
26 Kenned, P. M., R. J. Christopherson, and L. P.
MiUigan. 1976. The effect of cold exposure of
sheep on digestion, tureen turnover time and
efficiency of microbial synthesis. Br. J. Nutr.
36:231.
27 Kennedy, P. M., R. J. Christopherson, and L. P.
Milligan. 1982. Effects o f cold exposure on feed
protein degradation, microbial protein synthesis
and transfer of plasma urea to the rumen of sheep.
2747
Br. J. Nutr. 47:521.
28 Klopfenstein, T, R. Britton, and R. Stock. 1982.
Nebraska growth system. Page 310 in Protein
requirements for cattle: proceedings o f an in-
ternational symposium. F. N. Owens, ed. Oklahoma
State Univ., Stillwater.
29 Krishnamoorthy, U., C. J. Sniffen, M. D. Stern,
and P. J. Van Soest. 1983. Evaluation o f a rumen
dynamic mathematical model and in vitro simulated
rumen proteolysis to estimate rumen escape
nitrogen in feedstuffs. Br. J. Nutr. 50: 555.
30 Kropp, J. R., R. R. Johnson, J. R. Males, and F. N.
Owens. 1977. Microbial protein synthesis with low
quality roughage rations: isonitrogenous substitu-
tion of urea for soybean meal. J. Anim. Sci.
45:837.
31 Leng, R. A., and J. V. Nolan. 1984. Nitrogen
metabolism in the rumen. J. Dairy Sci. 67:1072.
32 Loerch, S. C., L. L. Berger, S. D. Plegge, and G. C.
Fahey, Jr. 1983. Digestibility and rumen escape of
soybean meal, blood meal, meat and bone meal
and dehydrated alfalfa nitrogen. J. Anita. Sci.
57:1037.
33 Mahadevan, S., J. D. Erfle, and F. D. Sauer. 1979.
A colorimetric m e t h o d for the determination o f
proteolytic degradation o f feed proteins by rumen
microorganisms. J. Anita. Sci. 48: 947.
34 Mahadevan, S., J. D. Erfle, and F. D. Saner. 1980.
Degradation o f soluble and insoluble proteins by
Bacteroides arnylopbilus protease and by rumen
microorganisms. J. Anita. Sci. 50: 723.
35 Mangan, J. L. 1972. Quantitative studies on
nitrogen metabolism in the bovine rumen. The rate
o f proteolysis of casein and ovalbumin and the
release and metabolism o f free amino acids. Br. J.
Nutr. 27:261.
36 Mathers, J. C., and E. L. Miller. 1981. Quantitative
studies of food protein degradation and the en-
ergetic efficiency of microbial protein synthesis in
the rumen of sheep given chopped lucerne and
rolled barley. Br. J. Nutr. 45: 587.
37 Mathison, G. W., and L. P. Milligan. 1971. Nitrogen
metabolism in sheep. Br. J. Nutr. 25: 351.
38 McAllan, A. B., and R. H. Smith. 1983. Estimation
of flows o f organic matter and nitrogen com-
ponents in postruminal digesta and effects of level
of dietary intake and physical form o f protein
supplement on such estimates. Br. J. Nutr. 49:119.
39 McAllan, A. B., and R. H. Smith. 1984. The
efficiency o f microbial protein synthesis in the
tureen and the degradability of feed nitrogen
between the mouth and abomasum in steers given
different diets. Br. J. Nutr. 51:77.
40 Merchen, N., T. Hanson, and T. Klopfenstein.
1979. Ruminal bypass of brewers dried grains
protein. J. Anim. Sci. 49:192.
41 Merchen, N. R., and L. D. Satter. 1983. Changes in
nitrogenous compounds and sites of digestion of
alfalfa harvested at different moisture contents. J.
Dairy Sci. 66: 789.
42 Miller, E. L. 1973. Evaluation o f foods as sources
o f nitrogen and amino acids. Proc. Nutr. Soc.
32:79.
43 MiSller, P. D., and K. V. Thomsen. 1977. Nitrogen
utilization from forages b y ruminants. Laboratorial
Journal o f Dairy Science Vol. 69, No. 10, 1986
2748 SATTER
and physiological measurements. Page 27 in
Quality of forage. Proc. Seminar organized by NJF.
Inst. Husdjurens Utfodring och yard. Rep. 54.
44 Nocek, J. E. 1985. Evaluation of specific variables
affecting in situ estimates of ruminal dry matter
and protein digestion. J. Anita. Sci. 60:1347.
45 Nolan, J. V., and R. A. Leng. 1972. Dynamic
aspects of ammonia and urea metabolism in sheep.
Br. J. Nutr. 27:177.
46 Nugent, J.H.A., and J. L. Mangan. 1978. Rumen
proteolysis of fraction I leaf protein, casein and
bovine serum albumin. Proc. Nutr. Soc. 37:48A.
47 Orskov, E. R., F. D. DeB. Hovell, and F. Mould.
1980. The use of nylon bag technique for evalua-
tion of feedstuffs. Trop. Anita. Prod. 5:195.
48 Owens, F. N., and W. G. Bergen. 1983. Nitrogen
metabolism of ruminant animals: Historical per-
spective, current understanding and future implica-
tions. J. Anim. Sci. 57 (Suppl. 2):498.
49 Pena-Castellanos, F. 1983. Heat treatment of
protein supplements for improving protein utiliza-
tion by dairy cows. Ph.D. Thesis, Univ. Wisconsin,
Madison.
50 Petersen, M. K., D. C. Clanton, and R. Britron.
1985. Influence of protein degradability in range
supplements on abomasal nitrogen flow, nitrogen
balance and nutrient digestibility. J. Anim. Sci.
60:1324.
51 Pichard, G. and P. J. Van Soest. 1977. Protein
solubility of ruminant feeds. Page 91 in Proc.
Cornell Nutr. Conf., Cornell Univ., Ithaca, NY.
52 Pilgrim, A. F., F. V. Gray, R. A. Weller, and C. B.
Belling. 1970. Synthesis of microbial protein in the
sheep's rumen and the proportion of dietary
nitrogen converted into microbial nitrogen. Br. J.
Nutr. 24: 589.
53 Poos. M. I., T. L. Hanson, and T. J. Klopfenstein.
1979. Monensin effects on diet digestibility,
ruminal protein bypass and microbial protein
synthesis. J. Anita. Sci. 48:1516.
54 Poos, Mary, T. Klopfenstein, and R. A. Britton.
1985. Evaluation of laboratory techniques for
predicting ruminal protein degradation. J. Dairy
Sci. 68:829.
55 Potter, G. D., J. W. McNeill, and J. K. Riggs. 1971.
Utilization of processed sorghum grain proteins by
steers. J. Anita. Sci. 32:540.
56 Prange, R. W., M. D. Stern, N. A. Jorgensen, and L.
D. Satter. 1984. Site and extent of protein diges-
tion in lactating cows fed alfalfa silage or baled
alfalfa hay. J. Dairy Sci. 67:2308.
57 Prigge, E. C., M. L. Galyean, F. N. Owens, D. G.
Wagner, and R. R. Johnson. 1978. Microbial
protein synthesis in steers fed processed corn
rations. J. Anita. Sci. 46:249.
58 Roffler, R. E., J. E. Wray, and L. D. Satter. 1986.
Production responses in early lactation to addition
of soybean meal to diets containing predominantly
corn silage. J. Dairy Sci. 69:1055.
59 Rook, J. A., I. M. Brookes, and D. G. Armstrong.
1983. The digestion of untreated and formal-
dehyde-treated soya-bean and rapeseed meals by
cattle fed a basal silage diet. J. Agric. Sci., Camb.
100: 329.
Journal of Dairy Science Vol. 69, No. 10, 1986
60 Roy, J.H.B., C. C. Balch, E. L. Miller, E. R. Orskov,
and R. H, Smith. 1977. Calculation of the N-
requirement for ruminants from nitrogen metab-
olism studies. Page 126 in Protein metabolism and
nutrition. Proc. 2nd Int. Symp. The Netherlands
Eur. Assoc. Anim. Prod. Publ. No. 22, Centre for
Agric. Pub. Doc., Wageningen.
61 Santos, K.A.S., M. D. Stern, and L. D. Satter.
1981. Ruminal protein degradation and amino acid
absorption in the small intestine of lactating cows
fed various protein sources. J. Anim. Sci. 55
(Suppl. 1):428. (Abstr.)
62 Schwab, C. G., L. D. Sarter, and A. B. Clay. 1976.
Response of lactating dairy cows to abomasal
infusion of amino acids. J. Dairy Sci. 59:1254.
63 Siddons, R. C., C. Arricastres, D. L. Gale, and D. E.
Beever. 1984. The effect of formaldehyde or
glutaraldehyde application to lucerne before
ensiling on silage fermentation and silage N diges-
tion in sheep. Br. J. Nutr. 52:391.
64 Stehr, D. 1984. Milk production response in
Holstein dairy cows fed protein supplements
relatively resistant to tureen microbial degradation.
M. S. Thesis, Univ. Wisconsin, Madison.
65 Stern, M. D., M. E. Ortega, and L. D. Satter. 1983.
Retention time in rumen and degradation of
protein supplements fed to lactating dairy cattle. J.
Dairy Sci. 66:1264.
66 Stern, M. D., L. M. Rode, R. W. Prange, R. H.
Stauffacher, and L. D. Satter. 1983. Ruminal pro-
tein degradation of corn gluten meal in lactating
dairy cattle fitted with duodenal T-type cannulae.
J. Anim. Sci. 56:194.
67 Stern, . M . D . , and L. D. Satter. 1982. In vivo
estimation of protein degradability in the rumen.
Page 57 in Protein requirements for cattle: pro-
ceedings of an international symposium. F. N.
Owens, ed. Oklahoma State Univ., StiUwater.
68 Tamminga, S. 1979. Protein degradation in the
forestomachs of ruminants. J. Anim. Sci. 49:1615.
69 Theurer, C. B. 1979. Microbial protein synthesis as
influenced by diet. Regulation of acid-base balance.
Church and Dwight Co., Piscataway, NJ.
70 Thomas, J. W., Y. Yu, T. Middleton, and C. Stal-
lings. 1982. Estimations of protein damage. Page
81 in Protein requirements for cattle: proceedings
of an internatinal symposium. F. N. Owens, ed.
Oklahoma State Univ. Stillwater.
71 van der Aar, P. J., L. L. Berger, G. C. Fahey, Jr.,
and N. R. Merchen. 1984. Effect of alcohol treat-
ments of soybean meal on ruminal escape of
soybean meal protein. J. Anim. Sci. 59:483.
72 Van Soest, P. J. 1982. Nutritional ecology of the
ruminant. O & B Books, Inc., Corvallis, OR.
73 Varga, G. A., and E. C. Prigge. 1982. Influence of
forage species and level of intake on ruminal
turnover rates. J. Anita. Sci. 55:1498.
74 Verite, R., M. Journet, and R. Jarrige. 1979. A new
system for the protein feeding of ruminants. The
PDI System, Livest. Prod. Sci. 6: 349.
75 Waldo, D. R. 1977. Potential of chemical pre-
servation and improvement of forages. J. Dairy Sci.
60: 306.
76 Weakley, D. C., M. D. Stern, and L. D. Satrer.
 SYMPOSIUM: PROTEIN AND FIBER DIGESTION 2749

1983. Factors affecting disappearance of feedstuffs
from bags suspended in the rumen. J. Anim. Sci.
56:493.
77 Whitlow, L. W. 1979. Rumen microbial degrada-
tion of feed protein. Ph.D. thesis, Univ. Wisconsin,
Madison.
78 Zinn, R. A., L. S. Bull, and R. W. Hemken. 1981.
Degradation of supplemental proteins in the
tureen. J. Anita. Sci. 52:857.
79 Zinn, R. A., and F. N. Ownes. 1983. Site of
protein digestion in steers: predictability. J. Anita.
Sci. 56:707.

Journal of Dairy Science Vol. 69, No. 10, 1986