Citrate-condensing Enzyme-Oxalacetate Binary Complex

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The purification of citrate-condensing enzyme.

The citrate-condensing enzyme was isolated as a crystalline protein from pig heart by Ochoa et al. (1). These workers reported that pig heart contained considerable quantities of the condensing enzyme. We were surprised when we obtained much higher yields of this enzyme from pig heart tissue with a different extraction procedure (2). This observation led to a purification procedure that yields ...

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Studies on the mechanism of the citrate condensing enzyme reaction.

Studies with deuterium as a tracer have shown that wheat germ and pig heart malic dehydrogenase act on the keto form of oxaloacetic acid (1, 2). The keto form of this acid has also been shown to arise in the enzymatic carboxylation of phosphorylenolpyruvate by wheat germ phosphoryl-enolpyruvate carboxylase (3) and by avian liver phosphoryl-enolpyruvate carboxylase kinase (2). In an attempt to e...

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Radiometric assay of citrate condensing enzyme (citrate synthetase) in liver tissue and mitochondria.

Citrate synthetase activity was determined in samples of commercially available citrate condensing enzyme. We measured the amount of radioactive citrate formed from the condensation of carbon-14 labeled acetyl CoA and oxaloacetate. The labeled citrate was oxidized by oxidative bromination; 14C02 evolved was collected and represented the amount of citrate synthesized. Enzyme activity as low as 1...

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Enzymatic synthesis of citric acid. I. Synthesis with soluble enzymes.

The synthesis of citrate from acetate, ATP,’ and oxalacetate by soluble enzyme preparations from pigeon liver was briefly reported in 1949 (1). CoA was found to be required for activity. Similar results were later reported by Novelli and Lipmann (2) with preparations from yeast and Escherichiu coli, and by Elliott and Kalnitsky (3) with kidney acetone powder extracts. It was further shown (1) t...

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The Citrate Cleavage Enzyme

This enzyme is widely distributed in animal tissues and has been partially purified from pigeon liver (1) and e.xtensively purified from chicken liver (2). Because of the complexity of the overall reaction, we attempted at first to fractionate the activity into more than one protein fraction. The results of these earlier studies led to the conclusion that one protein component or tightly bound ...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1966

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)96679-2