Isolation and characterization of multiple hamster hemoglobins.

Multiple hemoglobins were found in the peripheral blood of hamsters when separated by analytical isoelectric focusing in polyacrylamide gel between pH 6.0 and pH 8.0. Five of these hemoglobins (I-V) were present in sufficient quantities for isolation by preparative isoelectric focusing and subsequent characterization. Cellulose acetate electrophoresis of the isolated hemoglobins resulted in producing as many as six different globin chains. The five hemoglobins were further characterized by their amino acid composition, N-terminal amino acid residue, and molecular weight.