Pancreatic extracts from each of six different mammalian species including man, are shown to contain at least one anionic and one cationic variant of trypsinogen (trypsin). Additional isoenzymes of trypsin were detected in monkey, dog and rat pancreas. The ratios of enzyme activities determined in assays with synthetic N-benzoyl-DL-arginine pnitroanilide on the one hand, and the protein substrate Remazolbrilliant blue-hide on the other, indicate that anionic and cationic trypsins may possess widely different substrate specificities. The apparent specific activity of anionic trypsins for the synthetic substrate was found consistently higher than that of cationic isoenzymes. Differences also exist between similarly charged trypsins of different species. Rate assays for the trypsin in pancreatic extracts of juice, therefore,reflect the mean of tryptic activity of two or more isoenzymes with different substrate specificities and do not represent the real concentration of trypsin in the sample. The teleological significance of the existence of anionic and cationic species of trypsin in mammalian pancreas is unknown.

Keywords:
Enzymes, Trypsin, Trypsinogen, Specificity, Substrates, Determination
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1972
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