Study of lysosomal enzymes in fish muscle tissues - V : Partial purification of β-N -Acetylglucosaminidase in carp red muscle and their general property

概要

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The present study was undertaken to partially purify β-N-acetylglucosaminidase from carp red muscle and to examine their general property. β-N-Acetylglucosaminidase is separated by DEAE-cellulose chromatography into two components, lysosomal and soluble β-N-acetylglucosaminidase. The former consists of three isoenzymes, which have the optimum pH at 4.5 with citrate buffer and at 5.5 with acetate buffer. These enzymes are inhibited by acetate, N-acetylglucosamine and N-acetylgalactosamine. The latter has the optimum pH at 6-7 with both buffers and is inhibited by N-acetylgalactosamine only. The enzyme is easily denatured by incubation at 50 ℃ for 30 min. It is suggested that lysosomal β-N-acetylglucosaminidase is the type B enzyme of human serum and kidney reported by ROBINSON and STIRLING (1968) and that soluble β-N-acetylglucosaminidasemight be the type C enzyme of human and bovine brain reported by BRAIDMAN et al. (1974) and OVERDIJK et al. (1975)
三重大学水産学部の論文
1984-10-01