Abstract
Amounts of 1-anilino-8-naphthalene sulfonate (ANS) adsorbed by whole bovine erythrocyte and by its ghost membrane were studied at ANS concentration from 0.01 to 3mM. For whole erythrocyte the amount is nearly proportional to the free ANS concentration with the ratio of 1.1×10 [mole/l-packed-erythrocyte] / [mole/l-medium]. The ghost membrane has two kinds of binding site for ANS. The dissociation constants and the numbers of binding sites are calculated as follows : KI=9.1×10-5M and nI=1.9×10-2 mole/kg-membrane for site I ; KII=1.0×10-2 M and nII=5.8×10-1 mole/kg-membrane for site II. The binding site I and II can be attributed to protein and lipid, respectively, judging from membrane mass per mole of sites. The mechanism of disk to sphere transformation was discussed from these results.
