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- W2072301156 abstract "In accordance with what is observed for bovine or porcine chymotrypsinogens A and B, the activation of porcine chymotrypsinogen C and of Subunit II in bovine procarboxypeptidase A involves the specific cleavage by trypsin of the first basic bond in the N-terminal region. The short chain thus formed contains 13 residues instead of 15. The two missing residues correspond to an apparently characteristic deletion at positions 12 and 13. A comparison of the chains (N-terminal sequences) in six zymogens supports the view that bovine Subunit II is a chymotrypsinogen resembling more chymotrypsinogen C than chymotrypsinogens A and B. This suggests the existence in bovine and porcine pancreas of at least two related but distinct chymotrypsinogen lines." @default.
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- W2072301156 date "1969-05-01" @default.
- W2072301156 modified "2023-09-26" @default.
- W2072301156 title "Mode of activation and N-terminal sequence of subunit II in bovine procarboxypeptidase A and of porcine chymotrypsinogen C" @default.
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- W2072301156 doi "https://doi.org/10.1016/0005-2795(69)90229-3" @default.
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