ブタ小腸粘膜のペプチダ-ゼに関する研究--可溶性トリペプチダ-ゼの精製と若干の性質

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Tripeptidase [EC 3. 4. 1.3] in the cytosol fraction of hog small intestinal mucosa was purified by DEAE-cellulose column chromatography, Cellulofine GC-100 gel filtration, preparative electro-focusing, Sephadex G-150 gel filtration and affinity chromatography using Octylamino Sepharose 4 B. The overall procedure gave on approximately 12-fold purification, and the purified enzyme was found to be homogeneous by polyacrylamide gel electrophoresis. The molecular weight of this enzyme was estimated to be about 45, 000 by gel filtration. The optimum pH, optimum temperature and apparent Km value of this tripeptidase were 7.5, 45°C and 0.927 mM, respectively. Inhibition was found by the addition of pCMB and Hg2+, while no inhibition was found by EDTA and other metal chelating agents. Among the several tripeptides tested, Leu-Gly-Gly and Ala-Gly-Gly were hydrolyzed rapidly but Gly-Gly-Gly hydrolyzed slowly. No activity was found against dipeptides, acyltripeptide and tripeptideamide.
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