purification and properties of rat gastrocnemius muscle n-acetyl-i3-dglucosaminidase a and b.

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.