Abstract
Summary
The characteristics of binding of DDS and MADDS by HSA and of DDS by MPA have been studied by means of an equilibrium dialysis technique and analyzed by means of the Scatchard relationship. The plot of v/A vs v for each of the three studies yielded a straight line, suggesting only one species of binding site. Each molecule of HSA was found to possess one binding site for MADDS. Each molecule of MPA and HSA possessed 1/2 binding site for DDS, suggesting that DDS behaved as a bivalent molecule, and that one molecule of DDS was bound to two albumin molecules. The binding constant of HSA binding of MADDS was 10 times greater than the constant of HSA binding of DDS. The binding constants for DDS binding by both HSA and MPA were the same.
Get full access to this article
View all access options for this article.