Abstract
Exercise-associated protein (EAP) was purified to homogeneity from human serum after 10-km run and their properties were investigated. The purification was achieved by preparative polyacrylamide gel electrophoresis, anti-alb Sepharose chromatography, isoelectric focusing and gel filtration with high-performance liquid chromatography. The isoelectric point of the purified preparation was estimated to be 5.0, and the molecular weights in the absence and presence of 2-mercaptoethanol were respectively determined to be 25Kd on SDS-polyacrylamide gel electrophoresis. Amino acid analysis revealed a high content of glutamic acid and leucine and a low or no content of cysteine and isoleucine. Changes of their concentration in serum under various physical exercises were examined by rocket immunoelectrophoresis.
