BLOOD CELLS &

TRANSPORT OF
GASES
6A 2017
Ever heard of blood doping?
Functions of blood
■ Transport
■ Protective
■ Homeostatic
■ Heat distribution
■ Pressure provision
Typical blood smear
Fun blood facts

■ 8% of human weight (~5 kg)

■ 4-6 dm3 in adults
■ Connective fluid compound TISSUE
■ pH 7.35 – 7.45
The origin of
blood cells
 ERYTHROCYTES are…
■ SMALL
■ BICONCAVE DISCS (MAINTAINED BY CYTOSKELETON):
increased SA:Vol ratio
■ VERY COMMON (5 mill/mm3 of blood)
■ PRODUCED IN HAEOMOPOIESIS IN BONE MARROW (2-3
mill/sec) – controlled by ERYTHROPOIETIN (hormone from
kidney)
■ LIVE ~ 120 DAYS (WHY ONLY SO LONG?)
■ PMs BEAR MANY PROTEINS, GLYCOLIPIDS ON SURFACE (think
blood groups!)
■ NO MAJOR ORGANELLES WHEN MATURE
■ ABOUT 250 MILL MOLECULES OF Hb PER RBC (DENOTES RED
COLOUR) (90% of dry mass)
■ FLEXIBLE/EASILY CHANGES SHAPE
■ What is the big advantage of having Hb located in RBCs???
RECYCLING PROJECT!
■ PMs rupture
■ Haemoglobin split
into haem &
globin
■ Iron removed from
haem groups
(stored as ferritin
or reused)
■ Remainder of
haem groups
eliminated as bile
■ Globin split into
amino acids
Test yourself…explain these adaptations
for function
■ No nucleus
■ Contain Hb
■ Contain carbonic anhydrase
■ Round, disc-like shape
■ Biconcave shape
■ Thin, flexible PM
■ Act as containers
■ Small
The respiratory pigment
■ Increases
blood’s
oxygen-
carrying
capacity
■ Transports
about 98%
of oxygen
■ Has varying
affinity for
oxygen –
crucial
feature!
Haemoglobin
■ Reddish-purple without oxygen
■ Combines to form oxyhaemoglobin (brighter red)
■ Globular protein
■ RMM 68000
■ 4 polypeptide chains (level of protein structure?): 2 alpha, 2 beta
■ Conjugated protein – has prosthetic group (1 haem group PER
chain)
■ Each haem group can bind to ONE oxygen molecule (so how many
atoms?)
Oxygen dissociation
curves
Sigmoid shape
■ Hb has HIGH AFFINITY for oxygen where
concentration is high; LOW where it is low.
■ Exhibits COOPERATIVE BINDING (1st oxygen
molecule attaches with difficulty; distortion results in
progressively easier binding – ‘allosteric effect’)
■ AFFINITY CHANGES SUIT FUNCTION: Hb picks up
oxygen where provided; releases oxygen where
needed (bonds become unstable)
■ Degree of oxygenation of Hb is determined by partial pressure of
oxygen in surroundings
■ Partial pressure of a gas = measure of concentration of gas (aka
tension); pressure contributed by one gas to total pressure of a
mixture of gases
Terms to know

■ LOADING TENSION: pO2 producing 95% saturation of

haemoglobin
■ UNLOADING TENSION: pO2 producing 50% saturation of
haemoglobin
■ N.B. at partial pressure of 8 kPa, MOST Hb molecules are fully
saturated with oxygen
■ So DEGREE OF OXYGENATION OF Hb IS DETERMINED BY
OXYGEN TENSION IN IMMEDIATE SURROUNDINGS
■ What’s a
mud-
dwelling
worm to
do???
■ What is
the effect
of
shifting
the curve
to the
left?
■ Where
would a
llama’s
curve be?
What about a busy creature
like a shrew or a mouse?
■ CURVE TO LEFT:
■ INCREASED AFFINITY
■ INCREASED UPTAKE OF
OXYGEN
■ BECOME SATURATED
EVEN WITH LOW
PRESSURES OF OXYGEN
■ CURVE TO RIGHT:
■ REDUCED AFFINITY
■ INCREASED RELEASE OF
OXYGEN
■ LOWER SATURATION AT
ANY PARTICULAR
PRESSURE OF OXYGEN
What needs to happen when you are
active? What is the priority?
■ What’s going on here?
■ Presence of carbon
dioxide affects
properties of Hb…how?
■ How is this a
physiological
advantage?
Bohr effect
■ Say again
what is
going on?
■ NB. Both
oxygen and
carbon
dioxide
tensions
help to
make Hb
more
efficient –
combo deal!
Fetal Hb
■ What happens
when the
foetus is in the
womb?
■ How will the
baby obtain
oxygen from
the mother at
the placenta?
■ Hb differs! 2
alpha, 2 gamma
chains
Myoglobin:
the oxygen
store
■ How can you
tell that
myoglobin,
located in
mammalian
muscle cells,
is a major
oxygen
store?
■ What is its
purpose?
Can you see the
difference?
CARBON DIOXIDE TRANSPORT
The hydrogen carbonate ion route
10% travels as carbaminohaemoglobin
■ Carbon dioxide combines with the terminal amino groups of
some Hb molecules forming a neutral compound
■ Reversible reaction
So really blood is a great pH buffer!

■ In RBCs, Hb acts as a buffer forming haemoglobinic

acid
■ In the plasma, hydrogen carbonate ions combine with
protons to form carbonic acid
■ In plamsa, plasma proteins can join with protons to
form proteinic acid