S. Tayyab et Mk. Ali, BINDING OF BILIRUBIN TO MAMMALIAN ERYTHROCYTES, Comparative biochemistry and physiology. B. Comparative biochemistry, 118(1), 1997, pp. 97-103
Binding of bilirubin to erythrocytes of various mammalian species in t
he presence of their respective plasma albumins was studied at pH 8.0,
ionic strength 0.41 and at 37 degrees C. In human, buffalo, goat, and
sheep, the amount of erythrocyte-bound bilirubin increased with the i
ncrease in both the bilirubin/albumin molar ratio (B/A) and the total
bilirubin concentration. In all species, the binding patterns were qua
litatively similar. However, at any given B/A, goat erythrocytes bound
the highest amount of bilirubin, followed by buffalo and human erythr
ocytes; sheep erythrocytes bound the lowest amount of bilirubin. Incre
ase in erythrocyte-bound bilirubin per unit increase in bilirubin conc
entration at a constant BIA as obtained from the values of the slope o
f the plot between erythrocyte bound bilirubin and total bilirubin in
the incubate, was found to be highest for goat erythrocytes, followed
by buffalo, human, and sheep erythrocytes. At a given bilirubin concen
tration, percentage fractional binding of bilirubin between any two B/
As was found to be highest between 1.5 and 2.0, suggesting that a grea
ter amount of bilirubin was transferred from plasma to cells between B
/As 1.5 and 2.0. Percentage fractional binding of bilirubin was highes
t in goat erythrocytes, followed by buffalo, human, and sheep erythroc
ytes. These differences in the amount of erythrocyte-bound bilirubin w
ere not due to the effect of various plasma albumins. These results su
ggest that the difference in bilirubin binding by different mammalian
erythrocytes can be attributed to the difference in either the affinit
y of the erythrocyte receptors or their number or both. (C) 1997 Elsev
ier Science Inc.