Prolyl Endopeptidase form Bovine Testis : Purification, Characterization and Comparison with the Enzymes from Other Tissues

概要

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Pyolyl endopeptidase (EC 3.4.21.26) was purified from bovine testis by chromatographies on carboxymethyl (CM)-cellulose, diethylaminoethyl (DEAE)-Sephadex, hydroxyapatite, p-chloro-mercuribenzoate (PCMB)-Sepharose and Sephadex G-150. The enzyme appeared homogeneous as judged by disc gel electrophoresis. The molecular weight of the enzyme was estimated to be 76000 be gel filtration. The optimum pH of the activity was 7.2. The enzyme was inactivated with diisopropylphosphorofluoridate, Z-Gly-Pro-CH_2Cl, Z-Pro-prolinal and o-chloromercuribenzoate. The enzyme hydrolyzed biologically active peptides at the carboxyl side of prolyl residues. ALl of the characteristics of the testis prolyl endopeptidase are quite similar to those of the enzymes isolated from bovine brain, liver, kidney and muscle. These enzymes were immunologically indistiguishable : the antiserum raised against bovine brain enzyme a fused precipitation line against the enzymes from bovine testis, brain, liver and kidney, and the testis and brain enzymes gave the same immunoelectrophoretic profile.
公益社団法人日本薬学会の論文
1988-04-25