Curley G P, O'Donovan S M, McNally J, Mullally M, O'Hara H, Troy A, O'Callaghan S A, Dalton J P
School of Biological Sciences, Dublin City University, Glasnevin, Republic of Ireland.
J Eukaryot Microbiol. 1994 Mar-Apr;41(2):119-23. doi: 10.1111/j.1550-7408.1994.tb01483.x.
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+.
