Aminopeptidases from Plasmodium falciparum, Plasmodium chabaudi chabaudi and Plasmodium berghei

ABSTRACT. Using fluorogenic substrates and polyacrylamide gels we detected in cell-free extracts of Plasmodium falciparum, Plasmodium chabaudi chabaudi and Plasmodium berghei only a single aminopeptidase. A comparative study of the aminopeptidase activity in each extract revealed that the enzymes have similar specificities and kinetics, a near-neutral pH optima of 7.2 and are moderately thermophilic. Each has an apparent molecular weight of 80,000 ± 10,000, determined by high performance liquid chromatography on a calibrated SW500 column. Whilst the P. c. chabaudi and P. berghei activity co-migrate in native polyacrylamide gels, that of P. falciparum migrates more slowly. The three enzymes can be selectively inhibited by ortho -phenanthroline and are thus metallo-aminopeptidases; however, in contrast to other aminopeptidases the metal co-factor does not appear to be Zn²⁺.     

The Stimulation of Acid Phosphatase Activity in the Stalked Gland of Drosera rotundifolia

Localization of acid phosphatases (phosphomonoesterases II EC3.1.3.2 [EC] ) was studied in the secretory cells of stalked glandtissue of Drosera rotundifolia L. using a modified Gomori procedurewith p-nitrophenol phosphate (pNP) as substrate. In unstimulatedand 24 h stimulated tissue, some acid phosphatase activity waslocalized in vacuoles, cell wall regions and cuticular poresof only a few cells. Following stimulation for either 48, 72or 96 h, acid phosphatase activity was additionally observedin most gland cells within the nuclear envelope, endoplasmicreticulum and dictyosome cisternae and their associated vesicles,suggesting a de novo synthesis of acid phosphatases. Acid phosphatase, cytochemistry, Drosera rotundifolia, secretory cells