Abstract
Abstract The procyclic acidic repetitive protein (PARP) of Trypanosoma brucei was purified by cell fractionation followed by ion-exchange and concanavalin A-Sepharose affinity chromatography. PARP is membrane-bound and comprises about 1% of the total procyclic trypanosome protein or 6 x 10(6) molecules per parasite. The results of NH2-terminal sequencing and amino acid analysis indicate that PARP is processed by removal of an N-terminal signal sequence and the hydrophobic COOH terminus. Metabolic labeling of PARP with [3H] ethanolamine is consistent with attachment of the protein to the membrane via a glycosylphosphatidylinositol anchor. The glycolipid can be removed by base hydrolysis or nitrous acid deamination but is not susceptible to bacterial phosphatidylinositol-specific phospholipase C.
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