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Medical Journal of Islamic Republic of Iran، جلد ۳، شماره ۳، صفحات ۱۵۷-۱۶۴
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عنوان انگلیسی PURIFICATION AND PROPERTIES OF RAT GASTROCNEMIUS MUSCLE N-ACETYL-I3-DGLUCOSAMINIDASE A AND B.
چکیده انگلیسی مقاله 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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نویسندگان مقاله ja خان | ja khan
from the department of biochemistry, medical biology center, queen s university of belfast, bt97bl, northern ireland, united kingdom


مهرانگیز lewis | mhr lewis


نشانی اینترنتی http://mjiri.iums.ac.ir/browse.php?a_code=A-10-298-784&slc_lang=en&sid=en
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کد مقاله (doi)
زبان مقاله منتشر شده en
موضوعات مقاله منتشر شده Biological Sciences
نوع مقاله منتشر شده Original Research: Basic Science in Medicine
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