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Bulletin of the Korean Chemical Society (BKCS)

ISSN 0253-2964(Print)
ISSN 1229-5949(Online)
Volume 4, Number 3
March 20, 1983 

Isolation and Properties of β-N-Acetyl-D-glucosaminidase B from Rat Uterus
Jin-Ha Jung, Chul-Hak Yang
β-N-Acetyl-D-glucosaminidase B was highly purified with the following sequence of steps; DEAE-cellulose, CM-cellulose, and Sephadex G-200 gel filtration chromatograpies. The specific activity of the purified β -N-acetyl-D-glucosaminidase B was 2.2 units/mg protein with 12.9 % yield and 196.2 fold purity. The purified β-N-acetyl-D-glucosaminidase B showed single band on polyacrylamide gel electrophoresis. The final preparation of β -N-acetyl-D-glucosaminidase B was completely free friom arylsulfatase and β-glucuronidase. β -N-Acetyl-D-glucosaminidase B had pH optimum of 4.5 in 0.5 M sodium citrate buffer. The molecular weight of β-N-acetyl-D-glucosaminidase B was 133,000 by Sephadex G-200 gel filtration. The Km value of β-N-acetyl-D-glucosaminidase B using p-nitrophenyl-N-acetyl-β-D-glucosaminide as substrate was 1.0 mM and Vmax was 0.014 μ mole/min. β-N-Acetyl-D-glucosaminidase B was stable at 55℃ for 70 minutes. The crude β -N-acetyl-D-glucosamiinidase in 70 % ammonium sulfate retained 93 % activity after 7 months storage at -26℃. Bovine serum albumin, sodium chloride, and phosphate activated β -N-acetyl-D-glucosaminidase B. N-Acetyl-D-glucosamine, α-methyl-D-mannoside, and acetate inhibited β -N-acetyl-D-glucosaminidase B.
139 - 143
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