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

来源：

JOURNAL OF EUKARYOTIC MICROBIOLOGY | 1994年 / 41卷 / 02期

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

页码：119 / 123

页数：5

共 20 条

[1] LEUCINE AMINOPEPTIDASE FROM ARABIDOPSIS-THALIANA - MOLECULAR EVIDENCE FOR A PHYLOGENETICALLY CONSERVED ENZYME OF PROTEIN-TURNOVER IN HIGHER-PLANTS [J].