Identification of the parasite transferrin receptor of Plasmodium falciparum-infected erythrocytes and its acylation via 1,2-diacyl-sn-glycerol.

The transferrin receptor of schizont-infected erythrocytes of Plasmodium falciparum (Gambian clone FCR-3/A2) is a parasite-encoded protein of Mr 102,000, which is present in purified erythrocyte membranes. Polyclonal antiserum to the purified Mr 102,000 protein was raised in rabbits. At physiological pH, immunoaffinity-purified protein bound human ferrotransferrin but not apotransferrin.

Trypanosoma brucei variant surface glycoprotein has a sn-1,2-dimyristyl glycerol membrane anchor at its COOH terminus.

The membrane form of Trypanosoma brucei variant surface glycoprotein (mfVSG) is acylated with ester-linked tetradecanoic (myristic) acid (Ferguson, M. A. J.

Acylation of a Plasmodium falciparum merozoite surface antigen via sn-1,2-diacyl glycerol.

The 195-kDa merozoite protein synthesized in schizonts of Plasmodium falciparum (Holder, A. A., and Freeman, R.

Simultaneous reconstitution of Escherichia coli membrane vesicles with D-lactate and D-amino acid dehydrogenases.

Purified preparations of D-amino acid dehydrogenase [Olsiewski, P.J., Kaczorowski, G.