Purification of the mitochondrial citrate transporter in yeast.
We present a method of partial purification of mitochondrial citrate transporter of the yeast Saccharomyces cerevisiae. Based on functional evidence of interaction between citrate transport and citrate synthase, we have used an affinity column containing pig heart citrate synthase (PHCS) for the purification. The purified preparation shows two protein components whose Mr is approximately 50K and 60K. The specific activity of our purest fractions is 2.6 mumoles/min which compares favorably to that of purified beef liver enzyme and purified rat liver enzyme.
Persson
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Department of Veterans Affairs Medical Center, Dallas, TX.
Srere
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PA
D002352:Carrier Proteins / Q000737:chemistry / Q000276:immunology / Q000302:isolation & purification*; D002846:Chromatography, Affinity; D008081:Liposomes; D008928:Mitochondria / Q000201:enzymology*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D002352:Carrier Proteins; D008081:Liposomes; C020723:citrate-binding transport protein