1981 Volume 45 Issue 4 Pages 981-985
The specificity of highly purified carboxyl proteinase from Pycnoporus coccineus (formerly designated Trametes sanguined) was investigated with oligopeptides at pH 2.7. Hydrolysis of oxidized insulin peptide B1-B16 was observed at two peptide bonds (His10-Leu11 and Ala14-Leu15) during 3-hr incubation. The enzyme did not hydrolyze oxidized insulin peptide B15-B24. Hydrolysis of angiotensin (formerly designated angiotensin II) was observed at the Tyr4-Ile5 bond. Hydrolysis of proangiotensin (formerly designated angiotensin I) was also at the Tyr4-Ile5 bond. In conclusion, peptide bonds which have a hydrophobic amino acid in the P'1 position (as defined by Schechter and Berger, Biochem. Biophys. Res. Commun., 27, 157 (1967)) are preferentially cleaved by the trypsinogen activating carboxyl proteinase of Pycnoporus coccineus.
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