C H A P T E R
4 
Evaluation of Erythrocytes
N O R M A L ERY T H RO C Y T E S
Erythrocyte Morphology
Erythrocytes from all mammals are anucleated, and most are
in the shape of biconcave discs called discocytes (Figs. 4-1,
4-2).205 The biconcave shape results in the central pallor of
erythrocytes observed in stained blood films. Among common
domestic animals, biconcavity and central pallor are most pro-
nounced in dogs (Figs. 4-3, 4-4), which also have the largest
erythrocytes. Other species do not consistently exhibit central
pallor in erythrocytes on stained blood films. The apparent
benefit of the biconcave shape is that it gives erythrocytes high
surface area : volume ratios and allows for deformations that
must take place as they circulate. Erythrocytes from goats
generally have a flat surface with little surface depression;
a variety of irregularly shaped erythrocytes (poikilocytes) may
be present in clinically normal goats (Fig. 4-5). Erythrocytes
from animals in the Camelidae family (camels, llamas, vicuñas,
and alpacas) are anucleated, thin, elliptical cells termed ellip-
tocytes or ovalocytes (Fig. 4-6). They are not biconcave in
shape and are minimally deformable.437 Erythrocytes from
birds (Fig. 4-7), reptiles, and amphibians are also elliptical in
shape, but they contain nuclei and are larger than mammalian
erythrocytes. Blood cells in salamanders are the largest
recognized (Fig. 4-8).
Erythrocyte Functions
Mammalian erythrocytes normally circulate for several
months in blood despite limited synthetic capacities and
repeated exposures to mechanical and metabolic insults.
Erythrocytes have three functions: transport of oxygen (O2)
to tissue, transport of carbon dioxide (CO2) to the lungs, and
buffering of hydrogen ions (H+). In nonanemic animals, the
presence of hemoglobin within erythrocytes increases the
O2-carrying capacity of blood more than 50 times that of
plasma without erythrocytes. The O2 content of blood depends
on the blood hemoglobin content, the partial pressure of dis-
solved oxygen (PO2) in blood, and the affinity of hemoglobin
for O2.
Each hemoglobin tetramer is capable of binding four mol-
ecules of O2 when fully oxygenated. The initial binding of a
molecule of O2 to a monomer of tetrameric deoxygenated
hemoglobin facilitates further binding of O2 to the hemoglo-
bin molecule. The changing O2 affinity of hemoglobin with
oxygenation results in a sigmoid O2 dissociation curve (Fig.
4-9), when the percent saturation of hemoglobin with O2
is graphed against the PO2. The steepness of the middle
portion of the curve is of great physiologic significance
because it covers the range of O2 tensions present in tissues.
Consequently a relatively small decrease in O2 tension in
tissues results in substantial O2 release from hemoglobin.
The overall affinity of hemoglobin for O2 is decreased by
increasing H+, CO2, temperature, and, in most mammals,
2,3-diphosphoglycerate (2,3DPG). There is a direct correla-
tion between body weight and the O2 affinity of hemoglobin
in whole blood (lower body weight, lower O2 affinity) when
various species of mammals are compared.205
The O2 affinity of fetal blood is greater than that of mater-
nal blood except in the cat. Differences in fetal versus maternal
O2 affinity may potentiate O2 transport from the mother to
the fetus. However, the fetus is subjected to low arterial O2
tensions, and the increased O2 affinity of fetal blood is likely
needed to more fully saturate hemoglobin with O2.205
The ability of plasma to carry CO2 is small, but the car-
bonic anhydrase reaction in erythrocytes increases the CO2-
carrying capacity of blood 17-fold by rapidly converting CO2
to carbonic acid (H2CO3). The H2CO3 spontaneously ionizes
to H+ and bicarbonate (HCO3−). The HCO3− diffuses out of
the cell down a concentration gradient and chloride (Cl−)
moves in (chloride shift) to maintain electrical neutrality.
These processes are reversed at the lungs. Some CO2 is also
transported bound to hemoglobin as carbamino groups.
Deoxyhemoglobin binds about twice the CO2 that oxyhemo-
globin does.205
Hemoglobin is the major protein buffer in blood. Deoxy-
hemoglobin is a weaker acid than oxyhemoglobin. Conse-
quently, when oxyhemoglobin releases its O2 in the tissues,
the formation of deoxyhemoglobin results in increased binding
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