TY - JOUR T1 - PURIFICATION AND PROPERTIES OF RAT GASTROCNEMIUS MUSCLE N-ACETYL-I3-DGLUCOSAMINIDASE A AND B. TT - JF - MJIRI JO - MJIRI VL - 3 IS - 3 UR - http://mjiri.iums.ac.ir/article-1-1583-en.html Y1 - 1989 SP - 157 EP - 164 N2 - 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. M3 ER -