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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

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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.

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Authors and Affiliations

  1. Glycosphingolipid Research Group, Department of Biochemistry and Molecular Biology, School of Biological Sciences, University of Manchester, M13 9PT, Manchester, U.K.

    Martyn N Banks, Susan J Herbert & Colin H Wynn

  2. Protein Chemistry Group, John Curtin School of Medical Research, Australian National University, 2601, Canberra, ACT, Australia

    Colin H Wynn

Authors
  1. Martyn N Banks
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  2. Susan J Herbert
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  3. Colin H Wynn
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Banks, M.N., Herbert, S.J. & Wynn, C.H. Activator proteins for sulphatide hydrolysis and GM1-ganglioside hydrolysis. Probable identity on the basis of their co-purification, properties, ligand binding and immunochemical interactions. Glycoconjugate J 4, 157–170 (1987). https://doi.org/10.1007/BF01049453

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  • DOI: https://doi.org/10.1007/BF01049453

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