Elimination of CoASH interference from acetyl-CoA cycling assay by maleic anhydride.
A method for the removal of CoASH from tissue extracts by maleic anhydride is described. It eliminates CoASH interference in the acetyl-CoA cycling assay using phosphotransacetylase and citrate synthase. Maleyl-CoA thioether does not hydrolyze under the conditions of the assay and allows a reduction in the number of blank samples during acetyl-CoA determination. The levels of acetyl-CoA in whole rat brain, isolated synaptosomes, and mitochondria were found to be 61, 8.6, and 31.3 pmol/mg of protein, respectively.
Szutowicz
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A
Department of Clinical Biochemistry, Medical Academy, Gdańsk, Poland.
Bielarczyk
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H
D000105:Acetyl Coenzyme A / Q000032:analysis* / Q000592:standards; D000818:Animals; D001923:Brain Chemistry; D003065:Coenzyme A / Q000302:isolation & purification* / Q000592:standards; D008297:Male; D008299:Maleic Anhydrides; D008928:Mitochondria / Q000032:analysis; D010709:Phosphate Acetyltransferase; D051381:Rats; D011919:Rats, Inbred Strains; D013574:Synaptosomes / Q000032:analysis
D008299:Maleic Anhydrides; D000105:Acetyl Coenzyme A; D010709:Phosphate Acetyltransferase; D003065:Coenzyme A