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- W2093314260 abstract "By the use of glycyldehydrophenylalanine as assay substrate the peptidase was isolated from hog-kidney particulate material following solubilization with n-butanol. Purification techniques employed included ammonium sulfate fractionation, diethylaminoethyl-cellulose and carboxymethyl-cellulose chromatography, followed by Sephadex-gel filtration. The purified enzyme exhibited homogeneity in ultra-centrifugation and acrylamide-gel electrophoresis experiments. The molecular weight of the enzyme estimated by the approach-to-equilibrium method was 47 200. The zinc content of the purified enzyme measured colorimetrically and by atomic absorption spectroscopy was 1.36 μg Zn per mg protein indicating that the enzyme contains one atom of zinc per mole enzyme. Peptidase activity could be reduced by removal of zinc using o-phenanthroline dialysis and could be restored by dialysis against zinc-containing buffers. The enzyme catalyzed the hydrolysis of a variety of dipeptides including glycylglycine, L-leucylglycine, L-alanylglycine, and L-seryl-glycine; however, it did not promote the cleavage of L-leucylglycylglycine, L-alanyl-glycylglycine, L-serylglycylglycine, L-leucinamide or D-leucylglycine." @default.
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- W2093314260 date "1966-01-01" @default.
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- W2093314260 title "The purification and properties of a particulate renal dipeptidase" @default.
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- W2093314260 doi "https://doi.org/10.1016/s0926-6593(66)80046-2" @default.
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