Specificity and digestive function of alkaline proteinase from the gastric juice of the crayfish orconectes virilis
1970; Elsevier BV; Volume: 1; Issue: 1 Linguagem: Inglês
10.1016/0020-711x(70)90013-3
ISSN1878-6014
AutoresEdward J. DeVillez, John R. Lau,
Tópico(s)Peptidase Inhibition and Analysis
Resumo1. The oxidized B-chain of insulin was incubated in the presence of an alkaline proteinase isolated from the gastric juice of the crayfish. 2. Peptide maps of insulin digests indicate that the enzyme demonstrates broad proteolytic specificity. 3. Amino-acid analyses of peptide fragments obtained from insulin digests and incubations of the enzyme with some dipeptides of the same sequences as found in the B-chain suggest a preference for leucyl, tyrosyl, and phenylalanyl residues. 4. On die basis of its broad specificity, the alkaline proteinase is proposed as acting in a compensatory manner in that pepsin is not found in the gastric juice.
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