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Animal Reproduction and Physiology
Asian-Australasian Journal of Animal Sciences 1988;1(2): 99-106.
DOI: https://doi.org/10.5713/ajas.1988.99    Published online June 1, 1988.
Measurement of synthesis rate of long-chain acyl-coenzyme a ester in bovine liver by high-performance liquid chromatography
T. Mitsuhashi, M. Mitsumoto, Y. Yamashita, S. Ozawa
Abstract
A high performance liquid chromatographic procedure is described for the direct determination of the picomole amount of palmitoyl-Coenzyme A and stearoyl-Coenzyme A, using a stainless steel column packed with C-18 derivatized porous silica (5關m), an isocratic elution with a mixture of 33 mM KH2PO4/acetonitrile as a mobile phase and a UV detector. The long-chain acyl-Coenzyme A esters were determined in incubated microsomal fractions of a bovine liver to demonstrate the utility of this method for monitoring acyl-CoA synthesis in biological samples. The reaction rate of palmitate was higher than that of stearate. After a 60 minute incubation period, the generated amount of palmitoyl-Coenzyme A and stearoyl-Coenzyme A were approximately 70 and 20 n mol/mg micresomal protein, respectively. The advantage of this method are in that no decomposition of the CoA esters is involved, while the constituent molecular species is detected.
Keywords: HPLC; Acyl CoA; Bovine Liver


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