Glycosphinoglipid beta-galactosidases of cultured mammalian cells. Characterization of the enzymes from mouse cell line lmtk and human Lesch-Nyhan fibroblasts.
Evidence is presented for the existence of three distinct mammalian glycosphingolipid beta-galactosidase responsible for the hydrolysis of galactosylceramide, lactosylceramide and GM1 gangliside, respectively. Activity toward the (L-3-H)galactose-labeled substrates differed with respect to pH optimum, thermostability, effect of NaCl and inhibition by glycosides and related glycosphinglpids. Comparison of these enzymic acitivites in cultured mouse cell line LMTK- and human beta-galactosiddases could probably be detected in future experiments with somatic cell hybrids (formed by the fusion of these two cell strains by specifically inhibiting activity of mouse origin.
D000818:Animals; D002460:Cell Line; D002478:Cells, Cultured; D004355:Drug Stability; D005347:Fibroblasts / Q000201:enzymology; D005696:Galactosidases / Q000378:metabolism*; D005732:Gangliosides; D006027:Glycosides / Q000494:pharmacology; D006028:Glycosphingolipids; D006358:Hot Temperature; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D007926:Lesch-Nyhan Syndrome / Q000201:enzymology*; D051379:Mice; D009994:Osmolar Concentration; D012867:Skin / Q000201:enzymology; D012965:Sodium Chloride / Q000494:pharmacology; D012995:Solubility
D005732:Gangliosides; D006027:Glycosides; D006028:Glycosphingolipids; D012965:Sodium Chloride; D005696:Galactosidases