PURIFICATION OF THE RAT-LIVER MITOCHONDRIAL DICARBOXYLATE CARRIER BY AFFINITY-CHROMATOGRAPHY ON IMMOBILIZED MALATE-DEHYDROGENASE

被引：14

作者：

LANCARBENBA, J ^{[1
]}

FOUCHER, B ^{[1
]}

SAINTMACARY, M ^{[1
]}

机构：

[1] UNIV ROUEN,FAC SCI,INTRACELLULAR TRANSPORTS LAB,CNRS,URA 203,F-76821 MY ST AIGNAN,FRANCE

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | 1994年 / 1190卷 / 02期

关键词：

MITOCHONDRION; DICARBOXYLATE CARRIER; PURIFICATION; AFFINITY CHROMATOGRAPHY; MALATE DEHYDROGENASE; (RAT LIVER);

D O I：

10.1016/0005-2736(94)90076-0

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：

The dicarboxylate carrier of rat-liver mitochondria, extracted by Triton X-100 and partially purified by hydroxylapatite chromatography, was retained by malate dehydrogenase immobilized on Sepharose gel, and eluted with 0.4 M NaCl. SDS-polyacrylamide gel electrophoresis of the eluate showed a predominant peptide band with an M(r) of 28000. The purified protein, incorporated into liposomes, mediated a butylmalonate sensitive malonate(out)/malatei(in) exchange that was inhibited by p-chloro-mercuriphenylsulfonate. Sulfate, malate and phosphate decreased the rate of exchange. The highly purified protein displayed all the properties of the dicarboxylate carrier. Moreover, the results suggest a possible functional interaction between mitochondrial carrier protein and malate dehydrogenase.

引用

页码：213 / 216

页数：4

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