HYSTERESIS OF CYTOSOLIC NADP-MALIC ENZYME II FROM TRYPANOSOMA-CRUZI

被引：14

作者：

AVILAN, L ^{[1
]}

GARCIA, P ^{[1
]}

机构：

[1] UNIV LOS ANDES,FAC CIENCIAS,CTR INGN GENET,DEPT BIOL,MERIDA 5101,VENEZUELA

来源：

MOLECULAR AND BIOCHEMICAL PARASITOLOGY | 1994年 / 65卷 / 02期

关键词：

TRYPANOSOMA CRUZI; MALIC ENZYME; HYSTERESIS;

D O I：

10.1016/0166-6851(94)90074-4

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：

NADP-malic enzyme II, one of two isoenzymes of NADP-malic enzyme (EC 1.1.1.40) in Trypanosoma cruzi epimastigotes, presents hysteretic behavior that results in a kinetic lag in the reaction progress curve. The lag is affected by the malate, aspartate and oxalacetate concentrations in the assay mixture. This dependence suggests that hysteresis is due to an association-dissociation process influenced by the binding of these ligands to the enzyme. The enzyme was separated from NADP-malic enzyme I and purified 43-fold from a cell homogenate by a procedure involving column chromatography on DEAE-Sephacel and Cibacron-blue Sepharose. The molecular mass of the highly purified enzyme was determined as 126 kDa.

引用

页码：225 / 232

页数：8

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