The hemoglobin of amphibia: II. Characterization of the hemoglobin of Rana esculenta L. physicochemical properties and amino acid composition

Abstract The hemoglobin from adult male Rana esculenta L. has been purified by chromatography on carboxymethylcellulose. Some physicochemical properties of the hemoprotein have been studied, and its molecular weight (from the Scheraga and Mandelkern equation) and the reactive -SH group content have been determined. Rana esculenta hemoglobin has been resolved by starch-gel electrophoresis and by carboxymethylcellulose chromatography into five and three heme-containing components, respectively. The amino acid composition of unfractionated hemoglobin and the three chromatographically separated components was determined.