title: Specificity studies on the oligosaccharide neuraminidase of human fibroblasts.
abstract: Competition and thermal inactivation experiments with different potential natural substrates indicated that in homogenates of human fibroblasts one single enzyme is acting on both (alpha 2-3) and (alpha 2-6) sialosyl linkages of oligosaccharides and glycoproteins, but not of the ganglioside GM3. N-Acetylneuraminic and 2-deoxy-2,3-dehydro-N-acetylneuraminic acids are competitive inhibitors, whereas chondroitin 4-sulphate and the drug Suramin are potent inhibitors of undefined type.
mesh_terms: D002809:Chondroitin Sulfates / Q000494:pharmacology; D005347:Fibroblasts / Q000201:enzymology*; D006801:Humans; D007785:Lactose / Q000031:analogs & derivatives / Q000378:metabolism; D009439:Neuraminidase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D009844:Oligosaccharides / Q000378:metabolism*; D012794:Sialic Acids / Q000378:metabolism; D013379:Substrate Specificity; D013498:Suramin / Q000494:pharmacology
chemical_list: D009844:Oligosaccharides; D012794:Sialic Acids; D013498:Suramin; D002809:Chondroitin Sulfates; D009439:Neuraminidase; D007785:Lactose