Volume 3, Number 3 and 4 (11-1989)                   Med J Islam Repub Iran 1989 | Back to browse issues page


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KHAN J, LEWIS M. PURIFICATION AND PROPERTIES OF RAT GASTROCNEMIUS MUSCLE N-ACETYL-I3-DGLUCOSAMINIDASE A AND B.. Med J Islam Repub Iran. 1989; 3 (3 and 4) :157-164
URL: http://mjiri.iums.ac.ir/article-1-1583-en.html

From the Department of Biochemistry, Medical Biology Center, Queen s University of Belfast, BT97BL, Northern Ireland, United Kingdom
Abstract:   (1558 Views)
N-acetyl-B-D-Glucosaminidase was purified by affinity and ionexchange chromatography. Two major, A and B, and three minor intermediate forms were isolated and characterized. NAG-A and NAG-B were purified 440 and 1200 fold with final yields of 16 and 23 percent respectively. Each activity was represented by a single protein band. After 70 min preincubation at 55°C a loss of70% activity of NAG-A and 30% activity of NAG-B respectively was observed. Divalent metal ions had no significant effect on either enzyme activity. N-acetyl-D-glucosamine was determined to be a competitive inhibitor for both activities. The method of purification reported here will be of significance in providing larger quantities for the better understanding of both Tay-Sach's and Sandhoff's diseases.
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