Abstract
A serum glycoprotein whose content is increased in mice by the administration of an antitumor agent, PSK, and which migrates to the so-called LC region on polyacrylamide gradient gel electrophoresis, was purified by repeated ion-exchange column chromatography on DEAE-Sephadex A-50, chromatofocusing and gel filtration. The purified protein was identified as mouse haptoglobin, since its chemical composition, isoelectric point (4.1), molecular weight (94000) and subunit structure were found to be very similar to those of human haptoglobin. Furthermore, the purified protein formed a complex with hemoglobin and increased the peroxidase activity of hemoglobin.
