Apr 1, 1979

Partial purification and properties of citrate synthase from sea urchin eggs

Journal of Biochemistry
K Okabayashi, E Nakano

Abstract

Citrate synthase [EC 4.1.3.7] was purified from sea urchin eggs about 14-fold with a 23% yield, based on the activity of the crude extract. The molecular weight of the enzyme was about 100,000 as determined by gel filtration. The optimum pH was about 7.8 in 100 mM Tris-HCl. The apparent Km values for acetyl-CoA and for oxaloacetate were 33 and 3.2 muM, respectively. Monovalent and divalent cations inhibited the enzyme. Iodoacetamide, pCMB, EDTA, NaF, and dithiothreitol did not affect the enzyme activity. Oxaloacetate protected the enzyme against heat denaturation. Among nucleotides, ATP was the most potent inhibitor of the enzyme. The inhibition by ATP was competitive with respect to acetyl-CoA and mixed with respect to oxaloacetate.

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Mentioned in this Paper

Sodium Fluoride
Ribonucleotides
4-Chloromercuribenzenesulfonate
Ovum
Oxaloacetates
Oxo-Acid-Lyases
Acetyl Coenzyme A
Inhibitors
Sea urchin (invertebrate)
Gel Chromatography

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