Guinea pig plasma murinoglobulin. Purification and some properties

Abstract

Murinoglobulin, a newly identified mouse plasma protein resembling alpha-macroglobulins [Saito, A. & Sinohara, H. (1985) J. Biol. Chem. 260, 775-781], was also found in guinea pig plasma, and purified to homogeneity. Guinea pig murinoglobulin consisted of a single 180-kDa polypeptide chain containing about 18% carbohydrate. It inhibited the proteolytic activities of trypsin and thermolysin towards Remazol brilliant blue hide powder, but stimulated the amidolytic activities of trypsin and Staphylococcus aureus V8 protease towards small synthetic substrates. Heat treatment of murinoglobulin completely abolished the former activities, but partially retained the latter activities. The ability of guinea pig murinoglobulin to inhibit the proteolysis was much weaker than that of the mouse homologue. On interaction with trypsin, murinoglobulin underwent cleavage of one susceptible bond with concomitant unmasking of one thiol group. Methylamine treatment also released one thiol group per molecule.