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  • Title: Immobilization of fatty acyl-CoA synthetase: effect on its stability and substrate specificity.
    Author: Soeda S, Kishimoto Y, Hashimoto T.
    Journal: Biochem Int; 1986 Feb; 12(2):225-33. PubMed ID: 3964283.
    Abstract:
    Fatty acyl-CoA synthetase purified from rat liver microsomes was immobilized on either CNBr-activated Sepharose 4B or activated CH-Sepharose 4B, and the enzymatic activities of the syntheses of CoA esters from lignoceric acid (C24:0) and palmitic acid (C16:0) were studied and compared. The ratio of activities of the synthesis of lignoceroyl-CoA to palmitoyl-CoA increased 4.5 fold with CH-Sepharose, but only slightly with CNBr-Sepharose. The effects of a detergent and chaotropic agent on both substrates were significantly altered by the immobilization. The results of this study thus indicate that the stability and fatty acid specificity of fatty acyl-CoA synthetase are significantly affected by the physical state of the enzyme.
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