Specificity of Alkaline Elastase Bacillus on the Oxidized Insulin A-and B-Chains

The substrate specificity of alkaline elastase Bacillus from alkalophilic Bacillus sp. Ya-B was investigated using oxidized insulin A- and B-chains. Under time-limited cleavage, the initial cleavage site of the enzyme on the oxidized insulin A-chain and B-chain was at the leucinel3-tyrosinel4 bond a...

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Veröffentlicht in:Journal of biochemistry (Tokyo) 1988, Vol.104 (3), p.416-420
Hauptverfasser: Tsai, Ying-Chieh, Lin, Yu-Tzu, Yang, Yunn-Bor, Li, Ywan-Feng, Yamasaki, Makari, Tamura, Gakuzo
Format: Artikel
Sprache:eng
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Zusammenfassung:The substrate specificity of alkaline elastase Bacillus from alkalophilic Bacillus sp. Ya-B was investigated using oxidized insulin A- and B-chains. Under time-limited cleavage, the initial cleavage site of the enzyme on the oxidized insulin A-chain and B-chain was at the leucinel3-tyrosinel4 bond and the leucinel5-tyrosinel6 bond, respectively. When the cleavage was completed, three major cleavage sites and three minor cleavage sites on the A-chain, and five major cleavage sites and four minor cleavage sites on the B-chain were found. However, most of the peptides produced after complete hydrolysis of the A- or B-chain by the enzyme were composed of four to six amino acid residues. The results suggest that this enzyme cleaves the oxidized insulin A- and B-chains in a block-cutting manner.
ISSN:0021-924X
1756-2651
DOI:10.1093/oxfordjournals.jbchem.a122482