Abstract
Carnitine acyltransferase was purified to homogeneity from mung-bean ( Vigna radiata L.) hypocotyl mitochondria. The native enzyme has an apparent M r of 45000 as measured by gel filtration. SDS-PAGE revealed the same indicating a monomeric structure. The enzyme is active with short-and long-chain acyl-CoAs. The activity ratio determined for the substrate acetyl-CoA and palmitoyl-CoA remained the same throughout purification. The ability of the enzyme to use acetyl-CoA and palmitoyl-CoA as substrates is unique amongst the carnitine acyltrans-ferases characterized to date. Apparent K m values for the enzyme substrates acetyl-CoA, palmitoyl-CoA, and l-carnitine were: 8.5, 2.5 and 5 μM, respectively.
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