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The membrane-bound and released forms of the variant surface coat glycoprotein from Trypanosoma brucei have been purified to homogeneity by a new rapid method in the absence of detergents. The conversion of the membrane-bound form to the released form has been found to consist of the cleavage of a phosphodiester bond, distal to the phosphate, linking the protein to a phospholipid. We suggest that this linkage constitutes the normal mode of attachment of the protein to the outer leaflet of the plasma membrane.

Type

Journal article

Journal

The Journal of biological chemistry

Publication Date

04/1985

Volume

260

Pages

5179 - 5183

Keywords

Animals, Trypanosoma brucei brucei, Phosphates, Lanthanum, Hydroxylamine, Hydroxylamines, Glycoproteins, Variant Surface Glycoproteins, Trypanosoma, Membrane Proteins, Isoelectric Point, Molecular Weight