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albumin:
soluble proteins important in
homeostasis by
maintaining osmotic potential of blood
working with haemoglobin to act as acid-base
buffer to maintain the pH level of blood
plasma (cont.)
nutrients: glucose, amino acids, fatty acids, glycerol
and water-soluble vitamins (B and C)
mineral salts: in form of ions to regulate the osmotic
potential and pH of blood
metabolic wastes: include carbon dioxide, ammonia,
urea etc.
hormones and enzymes: for regulatory function
gases: oxygen and carbon dioxide
red blood cells (erythrocytes; red corpuscles)
number varies according to age, sex and state of
health
life span of 120 days; produced in haemopoietic tissue
(red bone marrow in adults; or liver in foetus) and
destroyed in the spleen or liver
biconcave discs → provide a larger surface area to
volume ratio for gaseous exchange
red blood cells (erythrocytes; red corpuscles)
cellis thin
→ efficient diffusion of gases
membrane is pliable
→ able to squeeze through small capillaries
→ ↑ contact with the capillary wall;
slow movement ensures complete exchange of
gases
enucleated (no nucleus) in mammals RBC (except
camel and llama)
→ more haemoglobin can be packed
contain enzyme carbonic anhydrase for transporting
carbon dioxide
white blood cells (leucocytes; white
corpuscles)
larger than RBC; present in smaller number
nucleated
important role in the body’s defence
mechanisms against disease
life span: normally a few days
2 main groups: granulocytes and
agranulocytes
granulocytes (polymorphonuclear / PMN
leucocytes)
granular cytoplasm
lobed nucleus
originate in the bone marrow
capable of amoeboid movement
neutrophils (phagocytes) (70%)
able to squeeze between the cells of the capillary walls and
enter the intercellular spaces, a process called diapedesis
actively phagocytic, engulf and digest disease-causing
bacteria
eosinophils (1.5%): cytoplasmic granules stained red
with red dye eosin; anti-histamine properties
basophils (0.5%): granules stained blue with basic dye
such as methylene blue; produce histamine and
heparin
agranulocytes (mononuclear leucocytes)
non-granularcytoplasm
monocytes (4%)
bean-shaped nucleus
actively phagocytic and ingest bacteria
lymphocytes (24%)
produced in the thymus gland and lymphoid tissue
small quantity of cytoplasm
temperature
oxygen and carbon dioxide
functions of blood
body defence
blood clotting to prevent excessive blood loss and
the entry of pathogens
phagocytosis by granulocytes
homeostatic function
maintenance of a constant blood osmotic potential
and pH (by plasma protein)
Transport of Oxygen
haemoglobin
265 million molecules of haemoglobin
protein molecule composed of four polypeptide chains
→ 2 α and 2 β chains → each is folded into globular
protein (globin) attached to a haem unit
each haem unit comprises of a porphyrin ring
containing an atom of iron (II) at the centre
each haemoglobin can carry 4 oxygen molecules
Hb + 4O2 ↔ HbO8 (oxyhaemoglobin)
Oxygen Dissociation Curve
oxygen concentration is measured by partial
pressure / oxygen tension → in kPa (kilopascals)
→ a measure of how much of the whole
atmospheric pressure is due to the oxygen
pressure
normal atm pressure = 100kPa or 760mmHg
21% of atm air = O2
∴ oxygen tension = 100 x 21% = 21kPa (or
152mmHg)
combination of oxygen with haemoglobin to form
oxyhaemoglobin occurs under condition when
the partial pressure of oxygen is high, such as in
the lung alveolar capillaries
when partial pressure of oxygen is low (in
tissues), oxyhaemoglobin tends to dissociate
and oxygen is released
affinity of oxygen to haemoglobin is measured
by determining the percentage of saturation of
blood with oxygen, which is determined by the
oxygen tension
when the percentage oxygen saturation of blood
is plotted against the partial pressure of oxygen
→ oxygen dissociation curve
loading tension: tension at which 95% of the
pigment is saturated with oxygen
unloading tension: tension at which 50% of the
pigment is saturated with oxygen
at partial pressure of oxygen = 0 → no oxygen is
attached to the haemoglobin
over the steep part of the curve, small decrease
in oxygen partial pressure → sizable fall in the %
saturation → oxygen given up
why S shaped?
allostery – when oxygen combines with iron (II)
atom, it distorts shape of haemoglobin slightly
→ facilitating much faster uptake of oxygen
blood can become fully saturated at relatively low
oxygen tension, i.e. haemoglobin has a high affinity
for oxygen
steep part of the curve: small drop in oxygen tension
→ comparatively large fall in blood saturation %
→ haemoglobin gives up more oxygen
high affinity for oxygen where oxygen tension is high
low affinity when oxygen tension is low
Bohr Effect
Bohr effect: increased partial pressure of
carbon dioxide
→ oxygen dissociation curve will be
shifted to the right
→ decrease the affinity of Hb for oxygen
∴ presence of CO2 facilitate the release of
O2 from Hb
curve shift to the right → release oxygen
more easily
curve shift to the left → load / pick up
oxygen more readily
myoglobin: another respiratory pigment; a
conjugated protein of a single polypeptide
with a single haem group; widely
distributed in animals and is particular
common in skeletal muscle tissues of
mammals, which is responsible for the
colour of ‘red’ muscle
curve for myoglobin is displaced to the left of
haemoglobin → great affinity for oxygen
it only begins to release oxygen when the partial
pressure of oxygen is below 20 mmHg
act as oxygen store in resting muscle tissue
release oxygen only when supplies of
oxyhaemoglobin have been exhausted, e.g. in
case of severe muscular exercises
if myoglobin-based oxygen is also exhausted,
muscle must respire anaerobically
why is the curve of foetus to the left of that of
mother?
the curve for foetus indicates that its blood has a
greater affinity for oxygen than the maternal
blood, as the foetus must obtain all of its oxygen
from its mother’s blood at the placenta
so, at any partial pressure of oxygen, the foetal
blood will take up oxygen from the maternal
blood and will always be more saturated with
oxygen than the maternal blood
how about the curve for small mammals and animals
living in high altitude like South America llama?
small mammals: shift to the right
large s.a. to vol. ratio
→ lose large amount of heat
→ higher metabolic rate to produce heat to
compensate for the loss which requires much
energy
→ more oxygen is released
llama: shift to the left
high altitude
→ reduced atmospheric pressure less oxygen
available (but still 21% of atm. air)
→ difficult to load haemoglobin with pressure
→ ∴ its blood has a high affinity for oxygen to
combine oxygen more readily
temp. ↑ → reduction in affinity of oxygen for
haemoglobin → ↑ dissociation of oxygen → curve
shift to the right → more oxygen is delivered to
the active region
carbon monoxide
the affinity of iron (II) for carbon monoxide is several
hundred times as great as for oxygen
a relatively stable compound called carboxy-
haemoglobin is formed
prevent oxygen from combining with haemoglobin
no longer possible for the transport of oxygen
death from asphyxia (shortage of oxygen)
Transport of Carbon Dioxide
in 3 ways
1. in aqueous solution in plasma (5%)
2. combined with haemoglobin to form
carbamino-haemoglobin (10%)
3. as hydrogencarbonate ion (85%)
Human Blood Groups – ABO system