Abstract
Bovine a-fetoprotein (AFP) was purified from bovine fetal serum in an overall yield of 10% of initial AFP content in the serum by DEAE Affi-Gel Blue chromatography and Chromatofocusing. The purified AFP was found to be a homogenous protein in two procedures used polyacrylamide gel electrophoresis and immunoelectrophoresis against rabbit anti-bovine AFP. These results suggest that the two chromatography systems are sufficient and reproducible for the purification of AFP in bovine serum.
