An Isolation Procedure for the Native α Chain of Bovine Hemoglobin.

In this paper we present a procedure for the isolation of the native bovine α chain. The method is based on affinity chromatography. The results show that the ligand-binding properties of the bovine α chain are almost identical to those of the human α chain. The hybrid α₂^B β₂^H prepared by mixing bovine α chains a human β chains shows ligand binding properties similar to those of human hemoglobin and different from those of bovine hemoglobin. [ABSTRACT FROM AUTHOR]