The proteolytic activities of chymopapain, papain, and papaya proteinase III

The three proteinases present in papaya latex: papain (EC 3.4.22.2) chymopapain and papaya proteinase III (EC 3.4.22.6), were standardized by active-site titration, and compared in proteolytic activity against azocasein, serum albumin and cartilage proteoglycan. The activities were all of the same order, although there were differences in pH dependence. SDS-polyacrylamide gel electrophoresis of the early products of digestion of albumin and phosphorylase a showed very similar patterns for the three papaya proteinases. Kinetic parameters for hydrolysis of benzyloxycarbonyl-phenylalanyl-arginyl-7(4-methyl)coumarylamide were determined for the three enzymes. Values for kcat/Km varied only within a factor of 2, but the individual constants were much higher for papain than for chymopapain and papaya proteinase III. In contrast to the results obtained with the synthetic substrate, the kinetic parameters for the initial hydrolysis of succinyl-albumin were very similar for the three papaya proteinases. This was consistent with their similar proteolytic activities in other assays.     

Antler anomalies in tule elk

Antler anomalies were evident in tule elk (Cervus elaphus nannodes) within 1 yr of reintroduction to Point Reyes, California (USA). These anomalies are consistent with previously described mineral deficiency-induced anomalies in cervids. The elk were judged deficient in copper. Low levels of copper in soils and vegetation at the release site, exacerbated by possible protein deficiency due to poor range conditions, are postulated as likely causes of the antler anomalies.