18 Functions of the Blood
CR. WEISS and W. JELKMANN
18.1 Basic Concepts
Blood is an opaque red fluid consisting of the
pale yellow plasma (called serum when the fi-
brinogen is removed) and the cells suspended in
it - the red corpuscles (erythrocytes), the white
corpuscles (leukocytes) and the platelets (throm-
bocytes). Blood has an important role in clini-
cal diagnosis, because it is easy to collect and
there are many diseases in which the blood com-
position and properties of the components are
characteristically altered.
Functions of the Blood
Transport. Blood is primarily a medium by which
substances are conveyed within the body. It
transports the respiratory gases oxygen and car-
bon dioxide both in physical solution and in
chemically bound form - O2 from the lungs to
the respiring tissues and CO 2 from the tissues
to the lungs. It moves nutrients from the places
where they are absorbed or stored to the sites
of consumption. The metabolites produced there
are transferred to the excretory organs or the
places where they can be further utilized. Blood
serves as a vehicle for the hormones, vitamins
and enzymes produced by the body itself, tak-
ing them up at the sites of production or stor-
age and carrying them - distributed throughout
the intravascular space - to their target organs.
Thanks to the high heat capacity of water, its
chief component, blood distributes the heat pro-
duced by metabolism and disperses it into the
environment by way of the lungs and respiratory
passages and the exposed body surface.
Homeostasis. As the blood circulates through the
body its composition and physical properties are
continually monitored by certain organs and, if
necessary, corrected so as to ensure constancy of
the internal milieu. This condition of homeostasis
- approximate constancy in the concentration of
dissolved substances, in temperature and in pH
- is a basic requirement for the normal functions
of all cells.
Prevention of hemorrhage. Another important
function of the blood lies in its capacity to coun-
teract bleeding by the closing of small injured
vessels and by coagulation (see pp. 419ff.).
Defense against foreign agents. The body is ca-
pable of making foreign bodies and pathogenic
organisms harmless; this ability is associated pri-
marily with phagocytic and antibody-forming
blood cells (see pp. 425ff.).
Blood Volume
Blood accounts for about 6-8% of the weight of
the body in adults, and in young children (be-
cause of their higher water content in general)
8-9%. In an adult this corresponds to a blood
volume of 4-6 liters (normovolemia). An above-
normal blood volume is called hypervolemia, and
a subnormal volume is hypovolemia. The way this
volume is measured is explained on p. 541, and
its distribution among the different parts of the
vascular system is described on p. 490.
Hematocrit
Definition and normal levels. The fraction of the
blood volume made up of erythrocytes is called the
hematocrit. In a healthy adult man it is 0.44-
0.46, and in a woman 0.41--0.43. In the clinic
hematocrit is still sometimes given in vol. %
(ml cells/dl blood). A healthy person exhibits
appreciable and maintained departures from this
value only when adapted to high altitudes. The
newborn hematocrit is about 20% higher, and
that of small children is about 10% lower than
that of women [6, 25].
To determine hematocrit (by Wintrobe's method) the blood,
having been prevented from clotting, is centrifuged for 10
minutes at about 1,000 g (g = relative acceleration due
Blood Plasma
to gravity) in standard hematocrit-tubes of small diame-
ter. The blood cells, having higher specific gravity than
the plasma, sink to the bottom; because the leukocytes
are lighter than the erythrocytes, they form a thin whitish
layer between the sedimented erythrocytes, and the plasma.
Because of the special flow properties of the erythrocytes,
the hematocrit values of the various organs differ, and
there are differences among the venous, arterial and cap-
illary values. The average whole-body hematocrit can be
derived by multiplying by 0.9 the hematocrit obtained for
cubital-vein blood with the Wintrobe method.
Hematocrit and viscosity of blood. Taking the vis-
cosity of water as 1, the mean relative blood vis-
cosity of healthy adults is 4.5 (3.5-5.4), and that
of the blood plasma is 2.2 (1.9-2.6). The internal
friction of the blood, its viscosity, increases more
than proportionally as the hematocrit increases
(cf. Fig. 20-3, p. 482).
Because resistance to flow rises linearly with vis-
cosity, any pathological increase in hematocrit
puts a greater load on the heart and can result in
inadequate circulation through certain organs.
18.2 Blood Plasma
A liter of human plasma contains 900-910 g of
water, 65 -80 g of protein, and 20 g of substances
of low molecular weight. The specific gravity of
plasma is 1.025-1.029; its pH varies slightly (7.37
-7.43) about a mean of 7.40 (arterial blood).
Fig. 18-1 is a diagram of the three great fluid
compartments in the body, the blood-vascular
system, the interstitial space (the spaces between
cells) and the intracellular space. The interstitial
fluid constitutes the environment of the mass
of cells in the body. By way of the large sur-
face of the capillary walls (highly permeable to
water and electrolytes) it exchanges substances
with the plasma. Because the exchange of wa-
ter and small molecules between plasma and
interstitial space is very rapid, the range within
which the composition of the interstitial fluid
can vary is small despite the considerable varia-
tions in uptake and release of substances by the
cells. For example, experiments with heavy water
(deuterium-labelled, D 2 0) have shown that over
70% of the plasma fluid is exchanged with the
interstitial fluid in one minute.
There are appreciable concentration differences
between plasma and interstitial space only with
respect to the proteins, for these molecules are
so large that they cannot pass readily through
the capillary membrane.
403
_ Stomach
~/ -
"':?~ pl.~. ~--:
mood
~-Kldney
--t-------'
31
-~
Skin
Interstitial
fluid
101
Intra=i
fluid
301
I
Internal __ Exchange
redistribution - with
environment
Fig. 18-1. Diagram of the fluid compartments in the body.
The volumes are indicated in round figures, for a person
weighing 70 kg. Modified from [8]
Plasma Electrolytes
Electrolyte concentrations. Table 18-1 and Fig.
18-2 summarize the ionic composition of plasma.
Among the substances in the group called simply
"organic acids" are lactic acid, the amino acids,
citric acid and pyruvic acid.
It is preferable no longer to give concentration as wIv ratio
(g/dl or mg/dl) but rather in terms of molarity (moljliter)
and normality or equivalent concentration (eqjliter =
mol/valence . liter). When it is necessary to allow for
the reduced volume of solvent in a solution in which the
dissolved particles require a great deal of space, molality
(mol/kg solvent) is often used as a measure of concentra-
tion (see Table 18-1).
Osmotic pressure. The concentration of dissolved
substances in the plasma can be expressed by
the osmotic pressure. That of normal plasma
is about 7.3 atm (5,600 mm Hg = 745 kPa) ,
which corresponds to a freezing-point depression
of -0.54°C. Solutions with the same osmotic
pressure as plasma are called isotonic, and by
the same convention hypertonic solutions have
higher, and hypotonic solutions lower osmotic
pressure. Plasma is isotonic with a barely 1/3
molal solution of a nonelectrolyte. 96% of the
osmotic pressure of blood is due to the presence
of inorganic electrolytes, mainly sodium chlo-
 404 18 Functions of the Blood

Table 18-1. Average concentrations of electrolytes and ride (crystalloid osmotic pressure). The molecu-
nonelectrolytes in human plasma lar weight of NaCI is low, so that there are many
g/1 meqj1 mmolfkg molecules per unit weight.
plasma Constancy of the internal milieu, or homeostasis,
water depends critically on regulation of the osmotic
Electrolytes pressure of the plasma. Any departure from the
Cations: normal extracellular osmotic pressure (plasma
Sodium 3.28 143 153 and interstitial fluid) causes a redistribution of
Potassium 0.18 5 5 water between the cells and their surroundings.
Calcium 0.10 5 3
Magnesium 0.02 2 1 Hypotonicity of the extracellular fluid causes in-
flux of water into the cells and hence swelling
Total 155
(cellular edema). Great increases in volume can
Anions: destroy the cell membrane (cf. osmotic hemolysis
Chloride 3.65 103 110 of erythrocytes, p. 413).
Bicarbonate 0.61 27 28
Phosphate 0.04 2 1
Hypertonicity, on the other hand, causes the cells
Sulfate 0.02 1 1 to lose water and shrink, so that the normal
Organic acids 6 tissue turgor is lost. In both cases the ability
Protein 65 to 80 16 ~1 of the cells to function is more or less severely
Total 155 impaired.
Non-electrolytes
Glucose 0.9-1.0 5 Functions of the plasma electrolytes. Isotonicity
Urea 0.40 7 of the suspension medium is one of the fun-
damental requirements for the maintenance of
function in isolated, surviving tissue. In itself,
however, it does not suffice to preserve cell func-
- tion; the various ions must be present in suitable
H~03 - proportions. Table 18-2 gives the composition
- HCO -
_ 3 of some "balanced" saline solutions which have
180 - Extracellular fluid proved useful as suspension media for living tis-
- sue in vitro. Although the different actions of
-H 2C03,
160 -
the various ionic species have long been known,
HCJ "
the mechanisms underlying these effects are not
- 3 understood in all details.
140 -
- HCd- 3

~
Q)
120 -
-
- K+
HPO~-
.):
Plasma Proteins

§. - ~,( :-<(~
General properties and functions. The high rela-
tive viscosity of plasma, 1.9-2.6 (water = 1), is
t::
0
-
~ 100
y

.,
'E
-j . "'.
almost entirely due to its protein content, 65-80
C,l
- Na+ CI - ~): .
.. ~
t:: I ~ Ii """'7""
80 -
0 GI- Na+
l)

@i SO~ Table 18-2. Composition of some commonly used sus-

- ~~: .

";{
,~ .~.
, - pension media. The numbers indicate the concentration
60 -
1"1 -v
,- (meqjl) of each ion.
- . Ringer Tyrode
40 - HPO~ -
r-r Pro-
Mg2+
Amphibians Mammals Mammals
,. :~~
:~{.
I
SO~- 'Iii¥' teln Na+ 115 Na+ 146 Na+ 149.4
~ Organ. ::..
)
HPO~-
K+ 1 K+ 4 K+ 2.7
20 ~ acids SO~-
K+
r-- Pro- Ca
Ca2~' ,.::......:....
K+ ._,
2+
(' h4:! Orgall. Ca2+
Cl-
2
106
Ca2+
Cl-
5.4
155.4
Ca2+
Mg2+
3.6
2.1
tein F"'= acids
Mg2~~ ~ M 2+'-,
g -- r- ,- Protein HCO;- 12 CI- 145.1
0 RCO;- 12.0
Plasma Interstitial Intracellular
(water) fluid RPO~- 0.7
Glucose 5.5
Fig. 18-2. Electrolyte composition of plasma, interstitial
(mmol!1)
fluid, and intracellular fluid. Modified from [8]
Blood Plasma
Albumin Hemoglobin y-Globulin
c::::> 0 these substances in solution. Their ability to bind
69,000 156,000
68,000
a-Lipoprotein P-Lipoprotein
0
p -Globulin
C ::::>
200,000
1,300,000
Rbrinogen
c:::::
400,000
,----,
10 nm 30nm
Fig- 18-3. Molecular weights and shapes (schematic) of
some plasma proteins and of hemoglobin. Modified from
[28]
g . 1-1. Because of the high molecular weight of
proteins, the molal concentration, as Table 18-
i shows, is considerably less impressive - only
about 1 mmol . kg-I. The protein fraction of
plasma is a mixture of many individually iden-
tifiable proteins. Their molecular weights range
from 44,000 to 1,300,000. Particles of this order
of magnitude are classified as colloids (Fig. 18-
3). The plasma proteins function in a number of
different ways.
1. Nutrition. The approximately 3 liters of plasma
in an adult's body carry about 200 g of protein
in solution, a convenient reserve supply. In gen-
eral the cells of the body take up not proteins
but rather their components, the amino acids;
however, certain cells - especially those of the
reticuloendothelial system (RES) - can take in
whole plasma proteins and break them down
by means of intracellular enzymes. The amino
acids thus produced diffuse into the blood and
are immediately available to other cells for the
synthesis of new protein.
2. Transport. Many small molecules (see pp.
408f.) are bound to specific plasma proteins dur-
ing transport from the intestine or storage or-
gans to the places where they are needed. The
large surface area of these proteins, with numer-
ous hydrophilic and lipophilic attachment sites,
makes them especially suitable to serve as ve-
405
hicles. By binding of their lipophilic groups to
water-insoluble fat-like substances they can hold
a large number of low-molecular-weight sub-
stances during their transport in the bloodstream
also assists in maintaining a constant osmotic
pressure.
3. Unspecific carrier function. All the plasma pro-
teins bind blood cations in a non-diffusible form.
For example, about 2/3 of the calcium present
in plasma is unspecifically bound to proteins.
This bound calcium is in equilibrium with the
physiologically effective, ionized calcium freely
dissolved in the blood. The binding of calcium
is pH-dependent, being enhanced at high pH
(alkalosis, p. 593).
4. Production of colloid osmotic pressure. The
contribution of the proteins to the total osmotic
pressure of the plasma is very small, because of
their low molecular concentration. Nevertheless,
the colloid osmotic (oncotic) pressure plays an
important role in regulating the distribution of
water between plasma and interstitial fluid. Be-
cause the capillary membranes are essentially
freely permeable to small molecules, the con-
centration of these molecules - and thus the
osmotic pressure associated with them - is ap-
proximately the same in the two fluids. But the
plasma-protein molecules are so large that they
encounter a relatively large resistance in passing
through the capillary wall (for example, isotope-
labelled albumin leaves the bloodstream with a
half-time of about 14 hours). This effect, com-
bined with the removal of protein by uptake into
cells and transport through the lymph, brings
about a protein concentration gradient between
plasma and interstitial fluid; the colloid osmotic
pressure in the plasma is ca. 25 mm Hg (3.3 kPa)
and that in the interstitial fluid is ca. 5 mm Hg
(0.7 kPa) , giving a difference of ca. 20 mm Hg
(2.7 kPa).
Any change in the osmotically effective concen-
tration of plasma protein disturbs the exchange
of substances and the distribution of water be-
tween blood and interstitial fluid. Because al-
bumin (see p. 407) represents the largest frac-
tion of the plasma protein (a relatively small
molecule, its molal concentration is about 6 times
higher than that of all the other plasma proteins),
changes in albumin concentration have an espe-
cially pronounced effect on colloid osmotic pres-
sure. Reduction of the plasma albumin concen-
tration often leads to retention of water in the
interstitial space (interstitial edema). Therefore
406 18 Functions of the Blood

artificial plasma solutions in general should have

the same colloid (and crystalloid) osmotic pres-
sure as the plasma. Polysaccharides (hydroxy- ~ Paper strip
ethyl starch, dextran) and polypeptides (gelatine)
Buffer solution
are usually used as the colloids, because it is
very expensive to extract human blood proteins
in pure form.

5. Buffer function. Because proteins are ampho- Albumin 59.2%

teric - able to bind H+ or OH- ions, depending ClI-Globulin 3.9%
on the pH - the plasma proteins act as buffers, Albumin CI2 -Globulin 7.5%
p -Globulin 12.1%
helping to keep the blood pH constant (see pp. y -Globulin 1 7 .3%
591f.).

6. Protection against loss of blood. The coagula-

bility of blood, which interferes with bleeding, is
based in part on the fibrinogen content of the Globulins
plasma (see p. 408). The process involv~s a chain p
of reactions in which a number of blood proteins
that act as enzymes cooperate, terminated by the
conversion of dissolved fibrinogen into the fibrin
meshwork of which the clot is composed (see pp.
419f.).

Fractionation of plasma proteins. Qualitative and

quantitative analyses of the plasma proteins are
carried out routinely (Fig. 18-4). Protein elec-
trophoresis is an important diagnostic aid, for
many diseases involve characteristic changes in
the plasma-protein spectrum.
Electrophoresis is the migration of electrically charged par-
ticles, dissolved or suspended in a fluid, along a voltage
gradient. Protein molecules are built up of single amino
acids joined together by peptide bonds. The electrolytic
nature of these molecules is derived in part from the ion-
ization of amino (-NH2) and carboxyl (-COOH) groups;
especially when these are present in side chains, they
are electrically charged in accordance with the pH of
the solvent (-NHj or -COO-). As far as the buffering
action is concerned, the pH-dependent imidazole groups
of the amino acid histidine (a major component of the
hemoglobin molecule) are even more significant.
The electrophoretic mobility of a protein is basically a
function of the applied voltage, the size and shape of the
molecule, and its electric charge, which depends on the
difference between its isoelectric point (IP) and the pH
of the solution. As can be seen in Table 18-3, the IPs of
the different plasma proteins are below pH 7 by varying
amounts. In neutral or alkaline solutions, then, the proteins
will migrate in the same direction, toward the anode, but
with different velocities (Fig. 18-4).
In another method of fractionation, which allows simul-
taneous determination of molecular weight, the ultracen-
trifuge (Svedberg) is used to generate accelerational forces
from 100,000 to 750,000 times the earth's gravity. For a
given centrifugal force, the rate of sedimentation depends
on the specific weight and the shape of the molecule (Fig.
18-3) and on the density of the suspension medium. In
density-gradient centrifugation the protein components of
G) -4.------------------------()
Fig 18-4. Electropherogram of human serum. The stained
bands on the paper strip (bottom) correspond to peaks
in the photometric curve, which represent the indicated
percentages of the various protein fractions. Top: diagram
of the apparatus for paper electrophoresis
a mixture can be especially well separated, for each be-
comes concentrated at a particular level in the tube.
A still more refined separation of plasma proteins can
be achieved with a combination of electrophoresis and im-
munoprecipitation. In this procedure, immunoelectrophore-
sis, electrophoretically separated protein fractions are al-
lowed to diffuse within a gel into a drop of antibody-
containing serum. When the protein antigen encounters
the serum, antibody precipitation occurs, and is evident
as a whitish zone of turbidity in the gel. In this way it
has been shown that electrophoretically uniform protein
fractions can consist of several immunologically distin-
guishable proteins (cf. Table 18-3).
Properties and functions of individual fractions.
Because electrophoresis is the analytical proce-
dure most commonly used, discussion will be
restricted to the components distinguishable by
this method. Fig. 18-3 shows diagrammatically
the size relationships and the shapes of the most
important plasma proteins.
Blood Plasma 407

Plasma albumin. About 60% of the total plasma
protein is albumin (35-45 g ,1- 1). With a molecu-
lar weight of 69,000, it is one of the smallest pro-
teins in the plasma. Because of its relatively high
concentration and the small size of the molecule,
it is responsible for almost 80% of the colloid
osmotic pressure of the plasma. The many small
molecules have a very large total surface area,
so that they are especially well suited to act
as carriers, binding a number of substances for
transport in the bloodstream. Among the sub-
stances bound by albumin are bilirubin, urobilin,
fatty acids, bile-acid salts and a few extraneous
substances such as penicillin, sulfonamides and
mercury. A single albumin molecule, for exam-
ple, can bind 25-50 molecules of bilirubin (MW
500) at a time. In many pathological states -
in particular, inflammatory diseases and cases of
liver and kidney damage - the amount of albumin
is reduced.
Plasma globulins. The term "globulin" designates
a group of electrophoretically separable compo-
nents. In order of diminishing mobility in the
electric field, these are called 1X1-, 1X2-, fJ - and
y-globulins (Fig. 18-4). Even these subfractions,
however, do not represent individual proteins.
With other procedures, such as immunoelec-
trophoresis, each can be further separated (Table
18-3).
The subgroup of lXI-globulins consists of a num-
ber of conjugated proteins, with carbohydrate
prosthetic groups predominantly in the form of
hexoses and hexosamines; these are called glyco-
proteins. About 2/3 of the glucose in the plasma
is bound as glycoprotein. This bound glucose is
not detected by clinical tests for blood sugar in
deproteinated plasma. It can be measured only
after it is released from the protein by acid hy-
drolysis, when its concentration is found to be 0.8
-1.65 g . 1- 1• This subfraction also includes an-
other group of carbohydrate-containing proteins,
the proteoglycans (mucoproteins); these contain
glucosaminoglycans (mucopolysaccharides).
Other proteins that migrate with the 1X1 group
are thyroxine-binding globulin, vitamin-B 12 -bind-
ing globulin (transcobalamin), bilirubin-binding
globulin, and cortisol-binding globulin (transcor-
tin);
In the IXrglobulin fraction there are haptoglobin,
which chemically is classified as a proteoglycan,
and the copper-containing ceruloplasmin. The
latter has 8 atoms of copper per molecule, which
are responsible for the oxidase activity of the
protein. About 90% of the total plasma copper
is bound to ceruloplasmin. However, the copper

Table 18-3. Protein fractions in human plasma. MW, molecular weight; IP, isoelectric point. From [15, 25, 27]
Protein fraction Mean concentration MW IP Physiological significance

Electro- Immunoelectro- gj1 Jlmolj1 ('10- 3 )

phoretic phoretic
Albumin Prealbumin 0.3 4.9 61 4.7 Binding of thyroxine; colloid
Albumin 40.0 579.0 69 4.9 osmotic pressure, vehicle
function; reserve protein
ill-globulins Acid ill-glycoprotein 0.8 18.2 44 2.7 Product of tissue degeneration?
ill-lipoprotein 3.5 17.5 200 5.1 Lipid transport (esp. phospho-
("high-density lipopro- lipids)
teins")
il2-globulins Ceruloplasmin 0.3 1.9 160 4.4 Oxidase activity, binds copper
il2-macroglobulin 2.5 3.1 820 5.4 Plasmin and proteinase inhibition
il2-haptoglobin 1.0 11.8 8.5 4.1 Binds hemoglobin to prevent loss
in urine
P-globulins Transferrin 3.0 33.3 90 5.8 Iron transport
p-lipoprotein 5.5 0.3 to 3,000 to - Lipid transport (esp. cholesterol)
("low-density lipopro- 1.8 20,000
teins")
Fibrinogen 3.0 8.8 340 5.8 Blood clotting
y-globulins IgG 12.0 76.9 156 5.8 Immunoglobulins: Antibodies
against bacterial antigens and
IgA 2.4 16.0 150 7.3 foreign protein
IgM 1.25 1.3 960 Isohemagglutinins
IgE 0.0003 0.002 190 - Antibodies (reagins)
408
transported in the bloodstream to the cells of
the body is bound to albumin rather than to
ceruloplasmin.
The p-globulins include the most important car-
rier proteins for lipids and polysaccharides. The
lipoproteins are of great functional significance
in that they can hold non-water-soluble fats and
lipoids in solution and act as a vehicle for their
transport in the blood. About 75% of all fats and
lipoids in the plasma are bound as lipoproteins.
Small amounts of lipoproteins are also found in
the lXI-fraction, but the majority migrate with the
/1-g10bulins. Of these, the most important is /11-
lipoprotein, a molecule of which can comprise as
much as 77% lipid. Analysis of the lipoprotein
mixture in the plasma by means of ultracentrifu-
gation and electrophoresis (the electrophoretic
mobility of the lipoproteins is due to their pro-
tein component) has become a useful tool in
diagnosis of the various forms of hyperlipopro-
teinemia (cf. textbooks of biochemistry). Apart
from the lipoproteins, the fraction comprises a
group of metal-binding proteins; one of these,
transferrin, serves as a carrrier of copper and,
most importantly, of iron. This metalloprotein
binds 2 (ferric) iron atoms per molecule, and is
the vehicle for iron transport in the blood. The
serum transferrin is normally only about 30%
saturated with iron (1 mg Fe3+ /1 serum).
The heterogeneous group of y-globulins includes
the proteins with the lowest electrophoretic mo-
bility; their isoelectric points, accordingly, are
nearer the neutral point than those of the other
plasma proteins (cf. Table 18-3). Among the
y-globulins are most of the protective and de-
fensive substances of the blood (immunoglobu-
lins; see p. 429). Because the demand for pro-
teins with such special functions varies, there
are wide fluctuations in the quantity and com-
position of the y-globulin fraction; in almost
all diseases, particularly the inflammatory ones,
the amount of y-globulins increases. The to-
tal amount of plasma protein in general re-
mains approximately the same, however, be-
cause the increase in y-globulins is accompanied
by a roughly equal decrease in albumin; the
so-called albumin-globulin ratio is reduced. The
erythrocyte-agglutinating substances anti-A and
anti-B are also y-globulins.
Fibrinogen appears as a narrow separate band,
between the /1- and y-globulin fractions. Fibrino-
gen is the dissolved precursor of fibrin, which
precipitates out of solution to form a blood
clot (see pp. 419ff.). Fibrinogen is an elongated
molecule with an axial ratio (length: width) of
17 : 1. The high viscosity of fibrinogen solutions
18 Functions of the Blood
results from the tendency of these molecules to
aggregate in a string-of-beads formation.
Characteristic changes in the fibrinogen fraction appear
only in a few rare diseases, so that there is little diag-
nostic value in electrophoretic demonstrations of altered
fibrinogen concentration. Moreover, the mobility of this
elongated molecule in paper electrophoresis is more de-
pendent on the kind of paper used than is that of the
other plasma proteins. For these reasons, serum rather
than plasma is usually used in clinical paper electrophore-
sis of blood proteins; the typical electropherogram shown
in Fig. 18-4 thus has no fibrinogen band.
Synthesis and turnover of plasma proteins. A hu-
man on a normal diet synthesizes about 17 g
albumin and 5 g globulin in 24 hours. The half-
life of albumin in the human is 10-15 days, and
that of globulin is about 5 days. That is, when
these times have elapsed 50% of the protein
present on the first day has been replaced by
newly synthesized protein.
Transported Plasma Components
As has been shown in the preceding sections,
the inorganic electrolytes and the proteins trans-
ported by the plasma critically affect, by their
very presence, its most important functional
properties. In this sense the inorganic electrolytes
and the proteins are functional elements of the
plasma.
There is another group of plasma components
which are simply transported and have little ef-
fect - within the physiological range of concen-
trations - on the characteristic physicochemical
properties of the plasma. For this heterogeneous
group of substances the plasma is first and fore-
most a means of transport. Among them are (a)
nutrients, vitamins and trace elements, (b) prod-
ucts of intermediary metabolism, (c) hormones and
enzymes, and (d) substances to be excreted.
Transported nutrients, vitamins and trace elements. The
largest fraction, by weight, of the nutrients transported
in the plasma is made up of lipids (all ether-soluble sub-
stances: fats, lipoids and steroids). The concentration of
these substances, however, fluctuates widely (Table 18-4).
After a very fatty meal the lipid content can rise to such
an extent (up to 20 g . 1- 1) that the plasma looks milky
white (lipemia). About 80% of the fatty acids are bound
to globulin as glycerides, phospholipids and cholesterol
esters (lipoproteins); most of the non-esterified fatty acids
form albumin complexes. In contrast to the plasma lipids,
the concentration of which depends on the momentary
metabolic state, the concentration of glucose, the most
important carbohydrate, stays relatively constant at 0.8
-1.2 g .1- 1 (4-7 mmol·I- 1 ) despite differences in uptake
and widely varying rates of utilization. Another group of
transported nutrients, the amino acids, are present in the