Bovine pancreatic elastase II cleaves Gln-Ile bond |
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Authors: | Azuma K Banshou Y Suzuki H |
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Institution: | (1) Division of Biosciences, Graduate School of Fundamental Life Science, Japan;(2) Department of Biosciences, School of Science, Kitasato University, Kitasato 1-15-1, Sagamihara-shi, Kanagawa-ken, 228-8555, Japan |
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Abstract: | A peptidase (GICP) that cleaves the Gln-Ile bond of a peptide Gly-Ile-Asp-Val-Gln-Ile-Tyr(T-1), a sequence in phenylalanine oxidase, was purified from bovine pancreas. The purified enzyme had an Mr of approximately 29,000, as determined by SDS-PAGE, and its N-terminal sequence was identical to that of bovine pancreatic elastase II. The enzyme released Gly-Ile-Asp-Val-Gln and Ile-Tyr from T-1 (Km = 8.3 M kcat = 2.1 s–1) and the catalytic efficiency (2.6 × 105 M–1s–1) was comparable to those of elastase II from porcine pancreas and rat mesenteric arterial bed perfusate. The P1 site specificity of GICP toward oxidized insulin A and B chains suggested that major cleavage sites were the peptide bond at the C-terminal side of Gln, Leu, His, and Tyr residues. |
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Keywords: | Bovine pancreas endopeptidase Gln-Ile bond serine protease elastase II substrate specificity |
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