The Basic Trypsin Inhibitor of Bovine Pancreas

A derivative of the basic pancreatic inhibitor which contained carboxamidomethyl groups on half-cystine residues 14 and 38 was incubated with trypsin and intact inhibitor at pH 5.5. The carboxamidomethyl derivative after separation from trypsin and intact inhibitor released only lysine when incubated with carboxypeptidase B. The derivative was oxidized with performic acid and a peptide corresponding to residues 1 through 15 in the inhibitor was isolated and identified. It was concluded that complex formation between this inhibitor and trypsin involves .cleavage of the peptide bond linking residues 15 and 16 (Lys-Ala).

• Publication year

  2001

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  Unknown venue

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• Identifiers
  DOI 10.1016/s0021-9258(18)93508-8
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  Open on Semantic Scholar

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  Semantic Scholar

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