title: Studies on the interaction of Clostridium perfringens sialidase with sialic acid linked to the internal galactose in monosialogangliotetraosyl ceramide.
abstract: Investigation of the action of highly purified Clostridium perfringens sialidase on ganglioside II3Neu5Ac-Gg4Cer and its oligosaccharide II3Neu5Ac-Gg4, in the presence and absence of sodium cholate, extend earlier results obtained with impure enzyme fractions. Sialidase labeled with 125I was found to bind to various ganglioside substrate micelles, including II3Neu5Ac-Gg4Cer, and to mixed ganglioside-sodium cholate micelles. No binding occurred between the enzyme and the ganglioside-derived oligosaccharide II3Neu5Ac-Gg4, even when radioactive II3Neu5Ac-Gg4-[3H]ol was used. The binding of sialidase to micellar substrate is a condition for enzymic hydrolysis. Correspondingly, II3Neu5Ac-Gg4Cer and II3Neu5Ac-Gg4Cer-sodium cholate micelles were hydrolyzed by the enzyme but II3Neu5Ac-Gg4 was not. Ganglioside oligosaccharide analogues containing an amino function at the reducing terminus or between two oligosaccharide chains, II3Neu5Ac-Gg4-NH2 and (II3Neu5Ac-Gg4)2NH, were hydrolyzed in the absence of cholate. A synthetic analogue of II3Neu5Ac-Gg4Cer containing only the fatty acid moiety and not the sphingosine residue (I1-deoxy-I1-stearamido-II3-monosialo-gangliotetraitol ) behaved as the ganglioside in the presence and absence of sodium cholate.
authors.forename: A P
authors.initials: AP
authors.lastname: Corfield
authors.forename: R
authors.initials: R
authors.lastname: Schauer
authors.forename: L
authors.initials: L
authors.lastname: Dorland
authors.forename: J F
authors.initials: JF
authors.lastname: Vliegenthart
authors.forename: H
authors.initials: H
authors.lastname: Wiegandt
mesh_terms: D055598:Chemical Phenomena; D002621:Chemistry; D019826:Cholic Acid; D002793:Cholic Acids / Q000494:pharmacology; D002850:Chromatography, Gel; D003016:Clostridium perfringens / Q000201:enzymology*; D005677:G(M1) Ganglioside / Q000378:metabolism*; D005690:Galactose / Q000378:metabolism*; D005732:Gangliosides / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D019158:N-Acetylneuraminic Acid; D009439:Neuraminidase / Q000378:metabolism*; D011485:Protein Binding; D012794:Sialic Acids / Q000378:metabolism*; D013379:Substrate Specificity; D013997:Time Factors
chemical_list: D002793:Cholic Acids; D005732:Gangliosides; D012794:Sialic Acids; D005677:G(M1) Ganglioside; D009439:Neuraminidase; D019826:Cholic Acid; D019158:N-Acetylneuraminic Acid; D005690:Galactose