Stimulation of GM3 ganglioside sialidase activity by an activator protein in patients with mucolipidosis IV and controls.
An activator protein that stimulates the enzymic hydrolysis of sialic acid from gangliosides by ganglioside sialidase was fractionated from human liver. This fraction was distinct from those stimulating the hydrolysis of galactose from GM1 ganglioside by beta-galactosidase and the hydrolysis of N-acetylgalactosamine from GM2 ganglioside by hexosaminidase A. This fraction was highly specific for the hydrolysis of sialic acid from GM3 ganglioside, and was equally effective in fibroblasts from patients with mucolipidosis IV and in fibroblasts from controls.
Ben-Yoseph
Y
Y
Department of Pediatrics, Wayne State University School of Medicine, Detroit, Mich.
Mitchell
D A
DA
Yager
R M
RM
Pretzlaff
R K
RK
D002855:Chromatography, Thin Layer; D003902:Detergents; D004789:Enzyme Activation; D005347:Fibroblasts / Q000201:enzymology; D005732:Gangliosides / Q000378:metabolism; D006801:Humans; D008099:Liver / Q000737:chemistry*; D009081:Mucolipidoses / Q000201:enzymology*; D019158:N-Acetylneuraminic Acid; D009439:Neuraminidase / Q000378:metabolism*; D012794:Sialic Acids / Q000378:metabolism; D012867:Skin / Q000166:cytology
D003902:Detergents; D005732:Gangliosides; D012794:Sialic Acids; C036052:GM3 ganglioside sialidase; D009439:Neuraminidase; D019158:N-Acetylneuraminic Acid