Studies on the interaction of zinc, cadmium and mercuric ions with native and chemically modified human serum albumin

Abstract

Zinc and Cd2+ ions combine with native human and bovine albumins on similar or identical sites. At pH 2.5-4*0, 130 g. ions of mercury combine with 105 g. of bovine albumin and 100 g. ions with 105 g. of human albumin. Evidence is produced to suggest that the binding of Zn2+ and Cd2+ ions to native albumin is governed by the electronegative charge on the molecule. The metal-ion-binding properties of albumins treated with bromoacetic acid and bromopropionic acid are reported.