STAGE-SPECIFIC EXPRESSION OF ALDOLASE ISOENZYMES IN THE RODENT MALARIA PARASITE PLASMODIUM-BERGHEI

被引：27

作者：

MEIER, B ^{[1
]}

DOBELI, H ^{[1
]}

CERTA, U ^{[1
]}

机构：

[1] F HOFFMANN LA ROCHE & CO LTD, DEPT PRTB, GRENZACHERSTR 124, CH-4002 BASEL, SWITZERLAND

来源：

MOLECULAR AND BIOCHEMICAL PARASITOLOGY | 1992年 / 52卷 / 01期

关键词：

GLYCOLYSIS; ALDOLASE ISOENZYME; EVOLUTION; PLASMODIUM-BERGHEI;

D O I：

10.1016/0166-6851(92)90032-F

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We have cloned two genes (aldo-1 and aldo-2) encoding the glycolytic enzyme aldolase of the rodent malaria parasite Plasmodium berghei. The amino acid sequence of one gene product, ALDO-1, is virtually identical to P. falciparum aldolase whereas ALDO-2, the second gene product, is different and has 13% sequence diversity to ALDO-1. We expressed ALDO-2 as an active enzyme in Escherichia coli and compared the biochemical and kinetic properties to that of P. falciparum recombinant aldolase (ALDO-1 type). Based on the K(m) and V(max) constants for FMP and FBP, neither ALDO-1 nor ALDO-2 can be clearly assigned to any of the known mammalian isoenzyme classes. We demonstrate that expression of the two isoenzymes is developmentally regulated: specific antibody probes detect ALDO-1 in sporozoite stages of P. berghei and ALDO-2 is found in blood stage parasites.

引用

页码：15 / 28

页数：14

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