Nature of the isozymes of rat liver mitochondrial malate dehydrogenase

Mann, Kenneth G.; Vestling, Carl S.

doi:10.1016/0005-2744(68)90148-4

Cited by 19 publications

(8 citation statements)

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“…In contrast, the mitochondrial enzyme is slightly basic and has a rather low net charge at neutral pH values, as shown by its low mobility during electrophoresis. This difference also applied to the two forms of malate dehydrogenase found in various other organisms and tissues (see e.g., Thorne et al, 1963;Thorne, 1968;Mann & Vestling, 1968). It is noteworthy that cytochrome c is also a basic protein.…”

Section: Discussionmentioning

confidence: 99%

“…In various tissues, including rat liver, there are two major forms of the enzyme, one exclusive to the cytoplasm and one to the mitochondria. These two forms have very different physical and chemical properties, but their substrate specificities are very similar (Thorne et al, 1963;Thorne, 1968;Mann & Vestling, 1968). Thus if both forms of the enzyme are synthesized at the same location, some mechanism must exist for the exclusive movement of one form into the mitochondrion while the other is released into the cytoplasm.…”

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Studies on the biosynthesis of mitochondrial malate dehydrogenase and the location of its synthesis in the liver cell of the rat

Bingham

Campbell

1972

Biochemical Journal

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A method is described for the isolation of mitochondrial malate dehydrogenase from either the whole tissue homogenate or from the microsomal fraction of rat liver. The procedure involves the treatment of the tissue extract with detergent followed by gel filtration and chromatography on Amberlite CG-50 and DEAE-cellulose. The resulting enzyme was homogeneous by the criterion of gel electrophoresis. Incubation of the microsomal fraction from rat liver under the usual conditions for protein synthesis in the presence of [(3)H]leucine resulted in the incorporation of (3)H into the mitochondrial malate dehydrogenase when purified as described. The results are taken to indicate that the mitochondrial enzyme is synthesized by the cytoplasmic ribosomes. Possible ways in which the cytoplasmic and mitochondrial forms of malate dehydrogenase reach their final locations in the cell are discussed.

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

Studies on the biosynthesis of mitochondrial malate dehydrogenase and the location of its synthesis in the liver cell of the rat

Bingham

Campbell

1972

Biochemical Journal

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“…Mann & Vestling (1968& Vestling ( , 1969& Vestling ( , 1970 demonstrated the somewhat variable presence during starch gel electrophoresis at pH 5.4 of two or three cathodic forms of m-MDH. They proposed an explanation based on the existence of dissimilar subunits which were shown to be capable of dissociating and reassociating under such conditions as brief exposure to low pH.…”

Section: Discussionmentioning

confidence: 99%

“…In addition, the procedure described produces enzymes with small, somewhat variable amounts of tightly complexed glycerophospholipids. and/or deamidation which led to the apparent modification of one of the two subunits but to no loss of maximum specific activity (Mann & Vestling, 1968.…”

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Rapid preparation of mitochondrial malate dehydrogenase from rat liver and heart

Kuan¹,

Jones²,

Vestling³

1979

Biochemistry

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Mitochondrial malate dehydrogenase (L-ma-1ate:NAD' oxidoreductase, EC 1.1.1.37) has been purified from both rat liver and rat heart by using Sepharose-Blue Dextran pseudoaffinity chromatography. Under the conditions employed most of the mitochondrial malate dehydrogenase and some cytosolic malate dehydrogenase are adsorbed, whereas many proteins simply pass through. The blue column is then subjected to several treatments which elute a variety of other proteins (notably residual cytosolic malate dehydrogenase and lactate dehydrogenase) which also have an affinity for the bound dye Cibacron Blue F3GA. Mitochondrial malate dehydrogenase is then eluted by forming an abortive ternary complex with reduced nicotinamide adenine dinucleotide-sodium D( +)-malate. Pooled active fractions are passed through a preequilibrated diethylaminoethyl-Sephadex column which retains contaminating proteins. The active fractions are concentrated, and residual contaminants are removed by very small stepwise pH changes on a CM-52 cellulose column. The procedure is mild and rapid and yields enzyme which is homogeneous by the applied criteria. In M i t o c h o n d r i a l malate dehydrogenase (m-MDH) has been isolated and partially characterized from various sources (Ochoa

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The Chemical Nature of Isoenzymes

Wilkinson¹

1970

Isoenzymes

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Nature of the isozymes of rat liver mitochondrial malate dehydrogenase

Cited by 19 publications

References 4 publications

Studies on the biosynthesis of mitochondrial malate dehydrogenase and the location of its synthesis in the liver cell of the rat

Studies on the biosynthesis of mitochondrial malate dehydrogenase and the location of its synthesis in the liver cell of the rat

Rapid preparation of mitochondrial malate dehydrogenase from rat liver and heart

The Chemical Nature of Isoenzymes

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