Studies on the activation of the enzymatic hydrolysis of sphingomyelin liposomes.
Two pH optima were observed for the hydrolysis of sphingomyelin liposomes by brain and fibroblast extracts; one at pH 4.2-4.5, the other at pH 7-8. The proportion of the acidic activity in fibroblasts was affected greatly by the culturing conditions. Both the acidic and neutral enzyme activities were deficient in Niemann-Pick Type A fibroblasts, suggesting that both were genetically related. Partially purified activators from normal as well as Gaucher disease spleen stimulated the hydrolysis of sphingomyelin, at both pH values, by fibroblast and brain extracts. After further purification by DE-52 and Sephacryl 200 column chromatography the Gaucher activator retained its ability to stimulate sphingomyelinase and was active as well towards beta-glucocerebrosidase and beta-galactocerebrosidase.
D000818:Animals; D001921:Brain / Q000201:enzymology; D002417:Cattle; D004789:Enzyme Activation; D005260:Female; D005347:Fibroblasts / Q000201:enzymology; D005776:Gaucher Disease / Q000378:metabolism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D008081:Liposomes / Q000378:metabolism*; D009542:Niemann-Pick Diseases / Q000201:enzymology; D011247:Pregnancy; D013108:Sphingomyelin Phosphodiesterase / Q000378:metabolism; D013109:Sphingomyelins / Q000378:metabolism*; D013154:Spleen / Q000032:analysis; D014020:Tissue Extracts / Q000494:pharmacology
D008081:Liposomes; D013109:Sphingomyelins; D014020:Tissue Extracts; D013108:Sphingomyelin Phosphodiesterase