@article{oai:mie-u.repo.nii.ac.jp:00005595,
 author = {Ueno, Ryuji and Horiguchi, Yoshishige and Morishita, Tatsuo and Takahashi, Takashi},
 journal = {三重大学水産学部研究報告 = Bulletin of the Faculty of Fisheries, Mie University},
 month = {Oct},
 note = {application/pdf, 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)},
 pages = {43--50},
 title = {Study of lysosomal enzymes in fish muscle tissues - V : Partial purification of β-N -Acetylglucosaminidase in carp red muscle and their general property},
 volume = {11},
 year = {1984}
}