Abstract
The substrate specificity of Serratia protease was determined using various synthetic substrates. The enzyme did not participate in the hydrolysis of di- and tri-peptides except benzoylglycylleucinamide which was split at a limited rate into hippuric acid and leucinamide. The enzyme action on larger peptides was also studied. The enzyme cleaved the gly-leu bond in eledoisin related peptide and the gly-phe bond in bradykinin. The enzyme split oxidized insulin B-chain at twelve different peptide bonds.
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CITATION STYLE
MIYATA, K., TOMODA, K., & ISONO, M. (1971). Serratia Protease. Agricultural and Biological Chemistry, 35(4), 460–467. https://doi.org/10.1271/bbb1961.35.460
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