Hemoglobin heterogeneity in the pike, Esox lucius, and isolation of a homogeneous component

The hemolysate of the pike, Esox lucius, contains multiple molecular forms of hemoglobin molecules. Analytical gel electrofocusing, disc-gel electrophoresis and gel filtration chromatography indicate that the hemoglobin heterogeneity may be due to different charge isomers with mol. wt values similar to that of the human. Ion exchange chromatography on CM-cellulose permits to separate a hemoglobin component in a pure form. Globin chains analysis of this fraction and their isolation was also reported.