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  • Title: Acyl-CoA ligases from rat brain microsomes: an immunochemical study.
    Author: Singh I, Bhushan A, Relan NK, Hashimoto T.
    Journal: Biochim Biophys Acta; 1988 Dec 16; 963(3):509-14. PubMed ID: 2973813.
    Abstract:
    Acyl-CoA ligase activities, solubilized from rat brain microsomes, were fractionated into three different peaks by hydroxyapatite chromatography. Based on physical and chemical properties, we suggested that peak A (pamitoyl-CoA ligase) and peak C (lignoceroyl-CoA ligase) were two different enzymes (A. Bhushan, R. P. Singh, and I. Singh (1986) Arch. Biochem. Biophys. 246, 374-380). We raised antibodies against purified liver microsomal palmitoyl-CoA ligase (EC 6.2.1.3) and examined the effect of this antibody on acyl-CoA ligase activities for palmitic, arachidonic and lignoceric acids in microsomal enzyme extract and different acyl-CoA ligase peaks from the hydroxyapatite column. In an enzyme activity assay system in microsomal extract, the antisera inhibited the palmitoyl-CoA ligase activity but had very little effect on the acyl-CoA ligase activities for arachidonic and lignoceric acids. This antisera inhibited the acyl-CoA ligase activities for these three fatty acids in peak A and had no effect on these activities in peak B or peak C. Western blot analysis demonstrated that antibody to liver microsomal palmitoyl-CoA ligase cross-reacted with only peak A (palmitoyl-CoA ligase), but not with peak B or peak C. This immunochemical study demonstrates that palmitoyl-CoA ligase does not share immunological determinants with acyl-CoA ligases in peaks B or C, thus demonstrating that palmitoyl-CoA ligase (peak A) is different from the arachidonoyl-CoA and lignoceroyl-CoA ligase activities in peaks B or C.
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