Release of the variable surface coat glycoprotein from Trypanosoma brucei requires the cleavage of a phosphate ester.
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.
D000818:Animals; D006023:Glycoproteins / Q000378:metabolism*; D019811:Hydroxylamine; D006898:Hydroxylamines / Q000494:pharmacology; D007526:Isoelectric Point; D007811:Lanthanum / Q000494:pharmacology; D008565:Membrane Proteins / Q000378:metabolism*; D008970:Molecular Weight; D010710:Phosphates / Q000378:metabolism*; D014346:Trypanosoma brucei brucei / Q000378:metabolism*; D014643:Variant Surface Glycoproteins, Trypanosoma
D006023:Glycoproteins; D006898:Hydroxylamines; D008565:Membrane Proteins; D010710:Phosphates; D014643:Variant Surface Glycoproteins, Trypanosoma; D019811:Hydroxylamine; D007811:Lanthanum