K. Inoue et al., BINDING OF SODIUM ALKYL SULFATES TO HUMAN ERYTHROCYTE STUDIED WITH A SURFACTANT ION-SELECTIVE ELECTRODE, Langmuir, 12(20), 1996, pp. 4644-4650
To clarify the mechanism of the shape change of human erythrocyte indu
ced by anionic surfactants, the binding of sodium alkyl sulfates (CnH2
n+1OSO3Na, n = 8, 10, 12) to human erythrocyte was studied. In the bin
ding experiments with surfactant ion selective electrodes, it was foun
d that all surfactants studied bound to the erythrocyte in two steps i
n the concentration range where the shape change occurred. From the an
alysis of binding isotherms, the binding constants (K-1, K-2) and the
total number of sites (n(1), n(2)) for each binding were obtained. K-1
is larger than K-2 for each surfactant; both K-1 and K-2 increase wit
h the number of the carbon atoms of the alkyl group of the surfactants
. These facts suggest that the first binding is stronger than the seco
nd binding and that the hydrophobic interaction between the alkyl chai
n of the surfactants and the erythrocyte is the main driving force for
each binding. Meanwhile, from the optical microscopic observation, it
was found that the echinocyte was induced only in the concentration r
ange of the second binding. Furthermore, to identify the binding sites
on the erythrocyte membrane for the surfactants, the differential sca
nning calorimetry (DSC) measurements of erythrocyte ghost were done, a
nd it was elucidated that the first binding site was the boundary lipi
d region of band 3 and the second binding site was the phospholipid la
yer of the erythrocyte membrane. These results imply that the shape ch
ange of the erythrocyte progresses via two steps of surfactant binding
, first, to the membrane protein, band 3, and second, to the lipid lay
er of the erythrocyte, and that the membrane proteins also play an imp
ortant role in the mechanism of the shape change of the erythrocyte.