Purification and characterisation of membrane-form variant surface glycoproteins of Trypanosoma brucei.
Membrane-form variant surface glycoprotein of Trypanosoma brucei can be prepared in the presence of para-chloromercuriphenylsulphonic acid. The membrane-bound enzyme that usually cleaves a lipid from this glycoprotein, thus producing the soluble variant surface glycoprotein, is inhibited by a range of sulphydryl reagents. The effect of such inhibitors, both on cell lysates and on semi-purified enzyme, reveals that the enzyme may have a sulphydryl at or near its active site. Fatty acid analysis and isoelectric point measurements of membrane form and soluble form are presented.
D002731:4-Chloromercuribenzenesulfonate / Q000494:pharmacology; D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D005227:Fatty Acids / Q000032:analysis; D006023:Glycoproteins / Q000302:isolation & purification*; D007525:Isoelectric Focusing; D008565:Membrane Proteins / Q000302:isolation & purification*; D014238:Trichloroacetic Acid; D014346:Trypanosoma brucei brucei / Q000032:analysis* / Q000201:enzymology; D014643:Variant Surface Glycoproteins, Trypanosoma
D005227:Fatty Acids; D006023:Glycoproteins; D008565:Membrane Proteins; D014643:Variant Surface Glycoproteins, Trypanosoma; D014238:Trichloroacetic Acid; D002731:4-Chloromercuribenzenesulfonate