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J. Biochem, 1988, Vol. 104, No. 3 416-420
© 1988 Japanese Biochemical Society

research-article

Specificity of Alkaline Elastase Bacillus on the Oxidized Insulin A-and B-Chains1

Ying-Chieh Tsai*, Yu-Tzu Lin*, Yunn-Bor Yang*, Ywan-Feng Li*, Makari Yamasaki** and Gakuzo Tamura**

*Institute of Biochemistry, National Yang-Ming Medical College Taipei, Taiwan, 11221
**Department of Agricultural Chemistry, The University of Tokyo Bunkyo-ku, Tokyo 113

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.

1This study was supported in part by a grant (NSC74-0412-B01O-24) from the National Science Council, Taiwan; and a grant from the Institute of Physical and Chemical Research, Japan.


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