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Activator proteins for sulphatide hydrolysis and GM1-ganglioside hydrolysis. Probable identity on the basis of their co-purification,properties, ligand binding and immunochemical interactions
Authors:Martyn N Banks  Susan J Herbert  Colin H Wynn
Institution:(1) Glycosphingolipid Research Group, Department of Biochemistry and Molecular Biology, School of Biological Sciences, University of Manchester, M13 9PT Manchester, U.K.;(2) Protein Chemistry Group, John Curtin School of Medical Research, Australian National University, 2601 Canberra, ACT, Australia
Abstract:The concurrent purification of the activator protein for sulphatide hydrolysis and for GM1-ganglioside hydrolysis including chromat ofocusing and hydrophobic chromatography stages is described. The purified preparation has a pl of 4.2 and the sub-unit Mr is 10 000. The stoichiometry of binding of sulphatide and ganglioside to the protein is very similar. Both activities are removed in similar proportions on binding to IgG purified from antisera raised against the activator protein. The probable identity of the activator protein for sulphatide hydrolysis with that for GM1-ganglioside hydrolysis and a molecular explanation for this identity are discussed.
Keywords:activators  sulphatide  ganglioside  Protein-glycosphingolipid interaction
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