Demonstration of the existence, and partial characterization, of a cell-surface beta-hexosaminidase from rat splenocytes.
Rat splenocytes are shown to exhibit cell-surface located beta-N-acetylglucosaminidase and beta-galactosidase activities. Preincubation experiments, solubilization experiments and chemical cross-linking experiments show that these enzymatic activities are indeed cell-surface localized. The solubilization and partial purification of the beta-N-acetylglucosaminidase activity is reported. Kinetic studies of the partially purified material with a variety of competitive inhibitors at several pH values suggest that at physiological pH the cell surface beta-N-acetylglucosaminidase may function as a carbohydrate binding protein rather than as a glycosidase.
D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003432:Cross-Linking Reagents; D006596:Hexosaminidases / Q000302:isolation & purification / Q000378:metabolism*; D007096:Imidoesters; D007700:Kinetics; D009596:Nitrophenols / Q000378:metabolism; D051381:Rats; D011917:Rats, Inbred Lew; D012995:Solubility; D013154:Spleen / Q000201:enzymology*; D001619:beta-N-Acetylhexosaminidases
D003432:Cross-Linking Reagents; D007096:Imidoesters; D009596:Nitrophenols; C029326:dimethyl pimelimidate; D006596:Hexosaminidases; D001619:beta-N-Acetylhexosaminidases