Ancient Fossils with

Preserved Soft Tissues

and DNA
Sean D. Pitman M.D.
Updated March, 2005
© May 2004

One of the earliest published

reports concerned DNA extracted

from ancient materials (i.e., greater

than one million years old) involved

Magnolia leaves (with intact

fragments measuring up to 820 base

pairs) found in lake bottom

sediments of Miocene age,

supposedly 17-20 million years old.3 This find was quite interesting because the

magnolia leaves were found in water logged clay deposits - i.e., they were still wet! Of

course, DNA disintegrates fairly rapidly when in contact with water (complete
disintegration in less than 5,000 years).33 Yet, this experiment was repeated with several

scientists reporting the retrieval of authentic plant cpDNA in the 700-1500 bp size

range.34,35

In commenting on the remarkably old DNA in the supposedly 17-million-year-old

magnolia leaf, Savante Pääbo exclaimed, "The clay was wet, however, and one

wonders how DNA could have survived the damaging influence of water for so long." 24

Good question. However, most of the supposedly "ancient" DNA which has been

recovered is from insects and plants preserved in dry amber, including a termite

estimated to be 25-30 million years old,2 a Hymenaea leaf thought to be 25-40 million

years old5 and a weevil estimated to be 120-135 million years old.1 The weevil DNA, in

particular, was once thought to be 80 million years older than any other DNA specimen

ever extracted and sequenced.

Even more amazing than this though are the findings of Dr. Cano, a microbiologist at

California State Polytechnic University. What Dr. Cano did was dissect a Dominican

stingless bee trapped in amber, which was thought to be 25 to 40 million years old.

What he found were very well preserved bacterial spores inside. In fact they were so

well preserved that they actually grew when placed in the right environment. In other

words, they were still alive! And, interestingly enough, their DNA closely matched the

DNA of modern bacteria that grow inside modern bees.26 Also, fairly recently, viable

bacterial endospores and proteobacteria were isolated from primary (halite) salt crystals

dated at over 250 million years old.30,36 The experiments were conducted in dedicated
clean laboratory facilities. So, contamination is thought to be unlikely in this case. So, of

course, the age of the crystals was subsequently questioned.33,37 Logically, since it

stretches the imagination that any form of living thing could remain viable for such long

periods of time, perhaps the dating methods used to date the crystals were wrong?

Good thinking! Also, it is interesting to note that the sequences from the study of

Vreeland et al. [ref. 30] show only 1–3 substitution differences from contemporary

bacterial sequences, whereas known mutation rates among related bacteria would have

suggested 59 differences.33

In this same line, the DNA extracted from amber, even though it was maintained in a

fairly dry environment, is also just as problematic as DNA sequences from ancient salt

crystals. R. John Parkes commented in Nature concerning this and other similar

phenomena by noting that, "There is also the question of how bacterial biopolymers can

remain intact over millions of years in dormant bacteria; or, conversely, if bacteria are

metabolically active enough to repair biopolymers, this raises the question of what

energy source could last over such a long period." 29

Regardless of these serious problems, such discoveries have been widely reported

by the media without remark regarding the difficulty that these finds present for the

standard geological time scale. DNA, like all other biological macromolecules, is

generally quite unstable and spontaneously breaks down - especially when hydrated or

"wet". In living cells, DNA is maintained by repair mechanisms, but after death DNA self-

destructs at a rather rapid rate. In a published review of the chemical stability of DNA,

Tomas Lindahl (1993) noted, “Deprived of the repair mechanisms provided in living

cells, fully hydrated DNA is spontaneously degraded to short fragments over a time
period of several thousand years at moderate temperatures”. Lindahl went on to argue

for the "contamination" of all such specimens by modern DNA suggesting that, "The

apparent observation that fully hydrated plant DNA might be retained in high-molecular

mass form for 20 million years is incompatible with the known properties of chemical

structure of DNA." 28 In a 1991 issue of Science Jeremy Cherfas expressed his

bewilderment noting, "That DNA could survive for such a staggering length of time was

totally unexpected - almost unbelievable." 25

In a similar vein, Sykes (1991) has commented that in vitro estimates of the rate of

spontaneous hydrolysis imply that no DNA would remain intact much beyond 10,000

years. In his review paper, Lindahl goes on to argue that, “It seems feasible that useful

DNA sequences tens of thousands of years old could be recovered, particularly if the

fossil has been retained at low temperature.” As an example Lindahl referred to DNA

from mammoth tissue thought to be 40,000 years old.

So, our knowledge of DNA stability makes it seem highly improbable that this

molecule could be preserved for more than a few tens of thousands of years at most.

Others have noted that, "Certain physical limits seem inescapable. In approximately

50,000 years, water alone strips bases from the DNA and leads to the breakage of

strands into pieces so small that no information can be retrieved from them. Oxygen

also contributes to the destruction of DNA. Even in ideal conditions–in the absence of

water and oxygen and at low temperature–background radiation must finally erase all

genetic information."27 Many other authors have suggested a "maximal DNA survival of

50 thousand (Kyr) to 1 million (Myr) years."33

 Yet, the fossils from which DNA has been recovered are thought to be, in some

cases, tens of millions of years old. There is obviously a problem here. It is for this

reason that some scientists are now viewing some of the reported finds (especially

those that do not involve preservation in amber) skeptically. It has been argued that

some of the detected residues were the result of contamination by modern DNA.33 For

example, "A recent large-scale study performed under strict aDNA conditions failed to

obtain endogenous DNA from amber insects despite the application of several different

extraction and PCR protocols. Even attempts to reproducibly amplify endogenous DNA

from the same extracts used in the original claim (i.e. from the 25–40 Myr amber

preserved bee) have failed. Additionally, parts of the reported 120–135 Myr weevil

sequence were subsequently shown to be of fungal origin and none of the amber

sequences passed relative rates tests."33 So, scientists have since been, or at least

have claimed to be, more conscientious in eliminated the possibility of contamination.

Regardless, all data suggesting the recovery of truly ancient DNA does not sit

comfortably with the accepted millions of years time scale.

Very Old Protein

Despite the reproducible evidence that DNA as well as many proteins are rather

unstable and decay relatively rapidly, the positive reported findings of such existent

material in fossils supposedly millions of years old, seems rather intriguing. For

example: In 1992, Dr. Muyzer, et al., used polymerase chain reaction (PCR) to amplify
a protein that they suspected to be osteocalcin from two Cretaceous dinosaurs

identified as “Lambeosaurus F38” (which they believe to be 75.5 million years old),

“Pachyrhinosaurus F39” (supposedly 73.25 millions years old), and a third dinosaur

sample identified only as “F33”. They used two different methods to determine if this

protein really was osteocalcin or not.

The first method used an immunological reaction. Here is how it works: When a few

molecules of a foreign substance are injected into an animal, that animal’s immune

system will naturally produce antibodies to fight it. The kind of antibodies it produces

depends on the kind of foreign material introduced. Furthermore, the animal’s immune

system will produce lots of antibody cells in response to just a few foreign molecules, so

the antibodies are much easier to detect than the foreign material itself.

The researchers took some osteocalcin from alligator bones and injected it into a

rabbit to see what kind of antibodies the rabbit produced to fight off the osteocalcin.

Then they took some powdered dinosaur bones and injected it into the rabbit, and it

produced the same kind of antibodies, indirectly indicating that there was osteocalcin in

the powdered dinosaur bones. The second method used a direct measurement of

Gla/Glu ratios “detected by high-performance chromatography.” 7

Their conclusion was that both methods showed osteocalcin was still present in the

three different dinosaur bones they analyzed. This was published in October, 1992. The

literature search found that all the articles on organic material still present in dinosaur

bones were published from April 1990 until November 1994 (As far as I can tell, there

has been nothing published in Nature or Science on the subject since then). In the

same publication as Dr. Muyzer 7, Dr. Matthew Collins made the following statement:
 "Dinosaurs hold an enduring fascination. We reported the detection of a protein in a

dinosaur bone, published at around the same time as the release of Steven Spielberg's

blockbuster, Jurassic Park, [so it] was bound to receive the full media treatment. Our

report claimed to have detected osteocalcin immunologically and also to have found an

unusual amino acid g-carboxyglutamic acid (Gla) in a dinosaur bone from immature

(unheated) sediments. Osteocalcin is peculiarly suited to such spectacular survival, it is

very abundant in bone, binds strongly to it and has the distinction of being the only

ancient protein ever to have been sequenced." 7

Some articles suggested that the finding had brought forward the chances of

successfully turning the science fiction of Jurassic Park into scientific fact. Elsevier

magazine (2/10/93) stated "[The detection of osteocalcin] has set other scientists

thinking, if it is possible for a protein, perhaps it is also possible for DNA". The Daily

Telegraph even suggested that trend-setting restaurateurs may start serving dinosaur

soup! The scientific community was more skeptical. Jeff Bada (an experienced protein

geochemist) warned in a 1992 interview in Science News, "I worry greatly about the

stability of Gla. Why would it remain unaltered for tens of millions of years?".

Scientists are asking, "How can this protein be so fresh when it is contained in such

old bones?" Perhaps we should consider the possibility that they will never find the

answer because they might be asking the wrong question. Maybe they should ask,

"How can these bones be so old when they contain such fresh protein?" That throws a

whole new light on the subject. They will not ever figure out how protein and DNA can
last for tens of millions of years without breaking down if protein and DNA cannot really

last for tens of millions of years. They might just as well be wasting their time.

Really "Old" Dinosaur Soft Tissues, Blood Cells, and

Protein

Many different kinds of

intact proteins are being

found in "ancient" fossils

that are not completely

fossilized. Some scientists

seem to have found intact

hemoglobin molecules in the

bones of 65 million-year-old

T. rex fossils! How fairly

large portions of such a

seemingly delicate molecule

could survive intact over

many millions of years is

quite a mystery.
 "The lab filled with murmurs of amazement, for I had focused on something inside

the vessels that none of us had ever noticed before: tiny round objects, translucent red

with a dark center. Then a colleague took one look at them and shouted, 'You've got red

blood cells. You've got red blood cells!'. It was exactly like looking at a slice of modern

bone. But, of course, I couldn’t believe it. I said to the lab technician: 'The bones, after

all, are 65 million years old. How could blood cells survive that long?'" 13,14

This account was given by Mary Schweitzer, a PhD student at the time, from

Montana State University. A well preserved Tyrannosaurus rex skeleton had been found

in 1990 and brought for analysis to Montana State University. During microscopic

examination of the fossilized remains, it was noted that some portions of the long bones

had not mineralized, but were in fact original bone. Upon closer examination it was

noted that within the vascular system of this bone were what appeared to be red blood

cells (note retained nucleus in the center of the apparent RBCs and the fact that reptiles

and bird generally retain the RBC nucleus while mammals, like humans, do not). Of

course, this did not seem possible since the survival of intact red blood cells for some

65-million years seems very unlikely if not downright impossible.

Further testing of these cells was done to attempt to disprove the notion that they

could possibly be red blood cells. Several analytical techniques were used to

characterize the material to include nuclear magnetic resonance (NMR), Raman

resonance and Raman spectroscopy (RR) and electron spin resonance (ESR). These

techniques did identify the presence of the heme group molecule, but the detection

limits of these methods were not able to rule-out or rule-in the presence of hemoglobin
or myoglobin proteins due to the small amount of specimen available. So, Schweitzer

and her team decided to use a more sensitive detection method, the immune system.

They injected some of the T. rex extract into laboratory rats to see if these rats would

mount an immune response to the foreign T. rex material. And, the rats did mount a

very specific immune response against hemoglobin. This immune response was not

only against heme, but hemoglobin, and not just hemoglobin in general, but against a

certain type of hemoglobin.42 The reaction was strongest against pigeon and rabbit

hemoglobin. There was also a weak reaction against turkey hemoglobin, but there was

no reaction against snake hemoglobin. The specificity of these reactions were further

confirmed by the lack of reactivity with plant and sandstone extracts.

Consider the conclusions that Schweitzer and her team made concerning these

findings:

"The production of antibodies specific for hemoglobin in two rats injected with the

trabecular extract is striking evidence for the presence of hemoglobin-derived peptides

in the bone extract. . . That the antisera did not react with snake hemoglobin shows that

the reactivity is specific and not artifact. . . When considered as a whole, the results

support the hypothesis that heme prosthetic groups and hemoglobin fragments were

preserved in the tissues of the Late Cretaceous dinosaur skeleton." 16

 These results are

quite interesting since

they indicate a very

specific immune

response, not just against

hemoglobin, but certain

types of hemoglobin

molecules. Note again

that the antibodies

formed did not react against snake hemoglobin indicating that the antibody reactivity

was "specific and not artifact." The question is, how much of the original T. rex

hemoglobin molecule would need to be intact to elicit such a specific immune response

in the laboratory rats?

Schweitzer goes on to suggest that "Immunogenicity is not dependent on fully

intact protein, and even very small peptides are immunogenic when complexed with

larger organic molecules . . . even after extensive degradation has occurred."42 But how

extensively, roughly, could the hemoglobin molecules have degraded and yet retain their

ability to elicit a fairly strong and quite specific immune reaction in laboratory rats? In

order to obtain such strongly specific immunogenicity it would seem that a significant

percentage of the globin portion of the hemoglobin molecule would need to be intact.

But, how could a protein of any significant size large enough to elicit such a specific

immune response be maintained over the course of 65 million years? One might very

reasonably conclude that natural decay, over this amount of time, would completely
destroy the ability of hemoglobin or the required larger fragments of degraded

hemoglobin from being antigenic in such a specific way.

The explanation for this phenomenon, given later by Dr. Horner (Schweitzer's

boss) and even Schweitzer herself, was that the tougher heme molecule survived the

65 million years with maybe three or four amino acids of the original globin molecules

attached to it. Consider the following statement Schweitzer made in a response to an

inquiry by Jack Debaun:

"But the heme itself is too small to be immunogenic [only about 652 daltons]. We

believe that there were possibly 3-4 amino acids from the original protein attached to

the heme, and that was what may have spiked the immune response." 17

Now, it just seems quite unlikely that

just 3 or 4 amino acids stuck onto a heme

group is going to give rise to an immune

response as specific for a certain type of

hemoglobin as was found in this case (Note

that a fully formed globin molecule ranges

from 141 to 146 amino acids in length with

specific folding characteristics that

antibodies detect). As far as I have been

able to tell, the degree of immune response specificity noted by Schweitzer et al. has

never been realized in any confirming experiment with so few hemoglobin amino acids
stuck to a heme group and I doubt that such an attempted experiment will ever be

successful.

There are several reasons why I feel this way. For one thing, a certain minimum

antigen size is required before it can elicit an immune response. The most potent

immunogens are macromolecular proteins with molecular weights greater than

100,000da (~740aa - Note: the average amino acid weighs ~135da). Substances

weighing less than 10,000da (~75aa) are only weakly immunogenic, and those foreign

proteins/antigens weighing less than 1,000da (~7aa) are usually completely non-

immunogenic. Homopolymers (repeats of the same amino acid) are pretty much non-

immunogenic regardless of size. Co-polymers of glutamic acid and lysine must be

~35,000da (~250aa) to be immunogenic. It seems then that, in general,

immunogenicity increases with structural complexity. Also, aromatic amino acids, such

as tyrosine or phenylalanine, contribute much more to immunogenicity than do non-

aromatic amino acids. For example, the addition of tyrosine to a co-polymer made up of

glutamate and lysine reduces the size limitation to ~15,000da (~100aa) and adding

tyrosine and phenylalanine together reduces the minimum to 4,000da (~30aa). Also, it

is all four levels of protein structure (1o, 2o, 3o, & 4o) that influence immunogenicity - not

just a short linear sequence of amino acids.18-21

Of course, a rather specific immune response can be elicited by relatively few

amino acids as part of an epitope on a larger protein molecule, but they usually are not

immunogenic without first being part of a larger molecule. Also, epitopes are not usually

sequential in nature but are assembled by protein folding. This means that a rather

large portion of the original molecule usually needs to be intact in order for most
epitopes to remain intact. Epitopes with definite three-dimensional shapes and charged

amino acids are particularly well recognized by antibodies. The average epitope

probably involves about 7 to 15 contact amino acid residues and a few of these may be

critical to the epitope's specificity and the avidity of the antibody-antigen reaction.18-21

But, in order to make an epitope antigenic, it must be processed first.

Antigen presenting cells (APCs) like macrophages, dendritic cells, and even B-

cells are responsible for antigen processing and the presentation of epitopes/antigens to

the T-cells. T-cells do not recognize the initial foreign antigen directly. They only

recognize processed parts of antigens, consisting of no more than 15 or so amino acids,

presented to them by APCs in association with MHC (major histocompatibility)

molecules. So, in order to activate T-cells (required for cellular immunity and very

helpful in humoral immunity), the foreign antigen must first be recognized as "foreign" by

the APC cells. This initial APC recognition requires more than just a handful of amino

acids floating around or else there would be complete meltdown of the immune system.

In fact, generally speaking, molecules with a molecular weight less than 10,000da

(~75aa) are only weakly immunogenic when picked up by APC cells. Significant

potency usually requires antigens to be rather large at over 100,000da (~750aa).22,23

Given all this, it seems quite difficult for me to imagine how "3 or 4" amino acids

stuck to a heme group could elicit an immune response that was so specific for a certain

type of hemoglobin. Recall that the heme molecule, by itself, only has a molecular

weight of around 652da. To make a strong as well as specific immunogen (such as the

strongly specific hemoglobin immunity developed in rats exposed to T. rex extract in this

case) one might expect the immunogenic hemoglobin molecule to be at least 10,000da
(~75aa or so) in size.18-21 Certainly then, a heme group with 3 or 4 amino acids attached

to it (just over 1,000da) would not seem to give rise to the relatively strong and specific

immune response (specific to a certain type of hemoglobin) observed by Schweitzer et

al. in rats exposed to T. rex bony extract.

However, the argument is sometimes used that Schweitzer failed to identify any

specific size of hemoglobin fragment by gel electrophoresis. What happened is that the

electrophoretic pattern observed by Schweitzer when she ran the T. rex proteins

through the gel was a diffuse or smeared pattern. This means that there were no

discrete clusters of proteins that were the same size. But this is only to be expected

since a wide range of protein sizes would only be expected after an extended period of

degradation. The fact of the matter is though that hemoglobin fragments ranging

between 30 and 200 amino acids in size where definitely present in the T. rex extract

(per NMR analysis filtering).16

Another argument often used is that the molecules that elicited the immune

response were indeed quite large, but they were made up of fragments of smaller

hemoglobin molecules and other organic and inorganic molecules to form a new

collective molecule. The problem here is that there is that this hypothesis has not been

tested or demonstrated. Beyond this it doesn't seem very likely. For one thing heme is

non-covalently bonded to the globin portion of the hemoglobin molecule. If the much

stronger covalent bonds were broken and rearranged so much between the remaining

amino acids, how is it reasonable that the relatively weak non-covalent bond between

the amino acids and the heme group would be maintained? Also, such rearrangement

of covalent bonds would have distorted the covalent bonds within the amino acids
themselves as well as between the covalent bonds they share with other amino acids.

This level of decay would alter the type of amino acids or destroy them as amino acids

completely. The specificity of the immune response against hemoglobin in particular

speaks strongly against this degree of change having taken place.

If this is not already

enough, Schweitzer recently

made an even more startling

discovery. About three years

ago (2002) she and her team

had to divide a very large T.

rex thigh bone in order to

transport it on a helicopter.

When the bone was opened

flexible, even elastic, soft

tissue "meat" was found

inside. This is incredible

because this bone was

supposed to be some 68

million years old. Microscopic

examination revealed fine

delicate blood vessels with what appear to be intact red blood cells and other type of

cells like osteocytes - which are bone forming cells. These vessels were still soft,

translucent, and flexible. Subsequent examination of other previously excavated T. rex

bones from this and other areas have also shown non-fossilized soft tissue preservation

in most instances.31

This find calls into question not only the nature of the fossilization process, but also

the age of these fossils. How such soft tissue preservation and detail could be realized

after 68 million years is more than miraculous - - It is unbelievable! Schweitzer herself

comments that, "We may not really know as much about how fossils are preserved as

we think . . .” 31 Now, if that is not an understatement I'm not sure what is.

So, it seems rather clear, despite the objections of many evolutionists, to include

Schweitzer herself, that a 1,000da molecule would elicit an extremely weak response at

best and

would not

necessarily

elicit a specific

response to a

certain type of

hemoglobin

molecule

since surface

epitopes are

generally

more specific in their antigenic nature than are buried epitopes (i.e., heme is somewhat

hidden within a cleft of the hemoglobin molecule so 3 or 4 amino acids attached to it

would also be somewhat hidden). How then is it remotely logical to suggest that a
molecule weighing just over 1,000da (a heme group plus 3 or 4 amino acids) could elicit

such a strong as well as specific immune response as Schweitzer et al. observed? In

light of the additional recent finds of even more striking soft tissue and blood cell

preservation, it seems much more likely that such an immune response so specific for

certain types of hemoglobin could only be elicited by a larger portion of intact

hemoglobin than many scientists seem to even consider. Of course, one can't really

blame them because explaining how delicate soft tissue vessels (with obvious red blood

cells inside containing relatively large portions of hemoglobin molecules) could remain

intact for over 65 million years seems just a little bit difficult.

All of this is a rather mute point, of course, in light of the fact that T. rex collagen

has been subsequently sequenced.

"I mean can you imagine

pulling a bone out the ground after

68 million years and then getting

intact protein sequences?" said

John Asara of Beth Israel

Deaconess Medical Center and

Harvard Medical School, lead

author of one of the studies. "That's just mind boggling how much preservation there is

in these bones."

The new finding will be viewed skeptically, admitted one of the researchers involved

in the two studies. "It's very, very, very controversial because most people have gone on
record saying there's an absolute time limit to anything that's protein or DNA," said Mary

Schweitzer, a molecular paleontologist at North Carolina State University.

Matthew Carrano, a dinosaur curator at the Smithsonian Institution in Washington,

D.C., who was not involved in either study, said the protein findings are robust. "Here

are the pieces of the protein. If you're going to refute this you have to explain how these

pieces got in there," Carrano said in a telephone interview. "It's not another molecule

mimicking the protein and giving off a similar signal. This is the actual sequence."32

Of course, despite this surprising turn of events, scientists do not question the

notion that the dinosaur bones really are tens of millions of years old. They still assume

the long ages and evolutionary relationship that they assumed before - as per the

following passages:

A comparison by Asara's team of the amino-acid sequence from the T. rex collagen

to a database of existing sequences from modern species showed it shared a

remarkable similarity to that of chickens. Amino acids are the molecular building blocks

of proteins; there are 20 of them used by organisms to build proteins, and their precise

order is determined by instructions found in DNA.

"I'm grateful that he was able to get the [amino acid] sequences out. That's the Holy

Grail," Schweitzer told LiveScience. . . Until now, family trees have been constructed

from the shapes of bones and teeth, a not-always-reliable technique."

 This finding supports the idea that chickens and T. rex share an evolutionary link

and bolsters previous research showing that birds evolved from dinosaurs and that birds

are living dinosaurs.

"Here we have a real molecule from a real dinosaur, and it's much more similar to a

bird than it is to anything else," Carrano said.32

Such finds are much more consistent with a fairly recent catastrophic burial within

just a few thousand years of time. Non-catastrophic burial would allow for rapid

biodegradation of such delicate soft tissues. Time itself destroys soft tissues as well as

DNA and proteins in short order. Current real-time observations suggest that bio-

proteins could not remain intact more than a few tens of thousands of years - 100,000

years at the very outside limit of protein decay. The fact that such proteins are found,

intact, in bones supposedly older than 65 million years is simply inconsistent with such

an assumed age - by a few orders of magnitude. For the same reason that the age of

ancient salt crystals thought to be 250 to 450 million years old was questioned when

living bacterial spores were discovered inside,33 the age of 65 million-year-old T. rex

bones should be questioned when intact elastic soft tissues and protein sequences are

found inside.

Carbon 14
 I think that one further study should be done. This study should be a Carbon 14

dating of this organic material as well as other “fossilized” organic material. If any

convincingly non-contaminant carbon 14 remains in any detectable amount in organic

specimens supposedly millions of years old, then a real problem arises that is

equivalent to finding a hominid in the Cambrian. This, combined with the fresh DNA and

protein problem seems to me to be quite a quandary for the theory of evolution. At least

I have not found a good solution advocated in the scientific literature to explain many of

these problems as of late.

1. Cano, R.J. et al. 1993. Nature363: 536-8.

2. De Salle, R. et al. 1992. Science257: 1933-6.

3. Golenberg, E.M. et al. 1990. Nature344: 656-8.

4. Lindahl, T. 1993. Nature362: 709-15.

5. Poinar, H.N. et al. 1993. Nature363: 677.

6. Sykes, B. 1991. Nature352: 381-2.

7. Muyzer, Gerard., Preservation of the Bone Protein Osteocalcin in Dinosaurs Geology,

Vol. 20, October 1992, pages 871-874.

8. D.C. Lowe, "Problems Associated with the Use of Coal as a Source of 14C Free
Background Material," Radiocarbon, 1989, 31:117-120.

9. Snelling A.A., Stumping Old-age Dogma. Creation, 1998, 20(4):48-50.

10. Snelling A.A., ‘Dating Dilemma,’ Creation, 1999, 21(3):39-41.

11. Vogel, Nelson and Southon, Radiocarbon, Vol. 29, No. 3, 1987

12. Giem PAL. 1997b. Carbon-14 dating methods and experimental implications. Origins
24:50-64.

13. M. Schweitzer and T. Staedter, 'The Real Jurassic Park', Earth , June 1997 pp. 55-57.
14. Morell, V., Dino DNA: The hunt and the hype, Science 261(5118):160–162, 9 July 1993.

15. Schweitzer Mary, Proceedings of the National Academy of Sciences, Vol. 94, p 6291.

16. Mary H. Schweitzer,* Mark Marshall, Keith Carron, D. Scott Bohle, Scott C. Busse, Ernst
V. Arnold, Darlene Barnard, J. R. Horner*, and Jean R. Starkey, Heme compounds in
dinosaur trabecular bone, Proc. Natl. Acad. Sci. USA, Evolution, Vol. 94, pp. 6291-6296,
June 1997 ( http://www.pnas.org/cgi/content/full/94/12/6291 )

17. Debaun, J. (http://www.televar.com/~jnj/item6.htm) - accessed Feb. 2004.

18. http://www.bio.davidson.edu/old_site/student/Lindthesis/Amy's%20Thesis.html

19. http://www.med.unc.edu/wrkunits/3ctrpgm/pmbb/mbt/GLOS.htm

20. http://bioweb.wku.edu/faculty/Davis/Biol328/Lecture5.html

21. http://www.coloradobiolabs.com/science.htm

22. http://sprojects.mmi.mcgill.ca/immunology/APC_text.htm

23. http://sprojects.mmi.mcgill.ca/immunology/spec_imm_cells.htm

24. Svante Pääbo, “Ancient DNA,” Scientific American, Vol. 269, November 1993, p. 92.

25. Jeremy Cherfas, “Ancient DNA: Still Busy after Death,” Science, Vol. 253, 20 September
1991, p. 1354.

26. Cano, Science, Research News, V.268, 5/19/95

27. Scientific American, 11/93, p.92

28. Tomas Lindahl, “Instability and Decay of the Primary Structure of DNA,” Nature, Vol. 362,
22 April 1993, p. 714.

29. R. John Parkes, “A Case of Bacterial Immortality?” Nature, Vol. 407, 19 October 2000,
pp. 844–845.

30. Russell H. Vreeland et al., “Isolation of a 250 Million-Year-Old Halotolerant Bacterium

from a Primary Salt Crystal,” Nature, Vol. 407, 19 October 2000, pp. 897–900.

31. Mary H. Schweitzer, Jennifer L. Wittmeyer, John R. Horner, Jan B. Toporski, Soft-Tissue
Vessels and Cellular Preservation in Tyrannosaurus rex, Science, March 25, 2005

32. Jeanna Bryner, T. Rex Related to Chickens, LiveScience ( Link ) Last Accessed: April 20,
2007; See also: Sharon Begley, T. Rex and His Family, Newsweek, April 23, 2007

33. Martin B. Hebsgaard, Matthew J. Phillip and Eske Willerslev, "Geologically ancient DNA:
fact or artefact?" TRENDS in Microbiology, Vol.13 No.5, May 2005 ( Link )

34. Soltis, P.S. et al. (1992), "An rbcL sequence from a Miocene Taxodium (bald cypress)",
Proc. Natl. Acad. Sci. U. S. A. 89, 449–451
 35. Kim, S. et al. (2004) "DNA sequences from Miocene fossils: An ndhF sequence of
Magnolia Latahensis (Magnoliaceae) and an rbcL sequence of Persea
pseudocarolinensis (Lauraceae)", Am. J. Bot. 91, 615–620

36. Fish, S.A. et al. (2002) "Recovery of 16S ribosomal RNA gene fragments from ancient
halite." Nature 417, 432–436

37. Hazen, R.M. and Roedder, E. (2001) "How old are bacteria from the Permian age?"
Nature 411, 155–156

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