Simultaneous purification by affinity chromatography of rat liver mitochondrial aspartate aminotransferase and malate dehydrogenase and electrophoretic properties

Mitochondrial aspartate aminotransferase and malate dehydrogenase were purified to homogeneity from rat liver by the use of aspartate-coupled Sepharose, ion exchange, and Blue Sepharose chromatography. This procedure permits rapid preparation of these enzymes. The p I of each enzyme was determined a...

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Published inAnalytical biochemistry Vol. 150; no. 2; pp. 332 - 336
Main Authors Crémel, G., Filliol, D., Waksman, A.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.11.1985
Subjects
affinity chromatography
Animals
aspartate aminotransferase
Aspartate Aminotransferases - isolation & purification
chromatography
Chromatography, Affinity
Electrophoresis, Polyacrylamide Gel
Isoelectric Focusing
isoelectrofocusing
liver
malate dehydrogenase
Malate Dehydrogenase - isolation & purification
Mitochondria, Liver - enzymology
Rats
isoelectrofocusing
malate dehydrogenase
chromatography
aspartate aminotransferase
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Summary:Mitochondrial aspartate aminotransferase and malate dehydrogenase were purified to homogeneity from rat liver by the use of aspartate-coupled Sepharose, ion exchange, and Blue Sepharose chromatography. This procedure permits rapid preparation of these enzymes. The p I of each enzyme was determined and anomalous electrophoretic properties of aspartate aminotransferase were described.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0003-2697
1096-0309
DOI:10.1016/0003-2697(85)90519-6