AMINOPEPTIDASES FROM PLASMODIUM-FALCIPARUM, PLASMODIUM-CHABAUDI CHABAUDI AND PLASMODIUM-BERGHEI

被引:45
作者
CURLEY, GP [1 ]
ODONOVAN, SM [1 ]
MCNALLY, J [1 ]
MULLALLY, M [1 ]
OHARA, H [1 ]
TROY, A [1 ]
OCALLAGHAN, S [1 ]
DALTON, JP [1 ]
机构
[1] DUBLIN CITY UNIV,SCH BIOL SCI,DUBLIN 9,IRELAND
关键词
MALARIA; METALLOPEPTIDASES; AMINOPEPTIDASES;
D O I
10.1111/j.1550-7408.1994.tb01483.x
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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 metalloaminopeptidases; however, in contrast to other aminopeptidases the metal co-factor does not appear to be Zn2+.
引用
收藏
页码:119 / 123
页数:5
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