Immobilization of fatty acyl-CoA synthetase: effect on its stability and substrate specificity.
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.
D000818:Animals; D000936:Antigen-Antibody Complex; D003066:Coenzyme A Ligases / Q000302:isolation & purification / Q000378:metabolism*; D003902:Detergents / Q000494:pharmacology; D004355:Drug Stability; D004800:Enzymes, Immobilized / Q000378:metabolism*; D007106:Immune Sera; D007700:Kinetics; D008862:Microsomes, Liver / Q000201:enzymology*; D017830:Octoxynol; D011092:Polyethylene Glycols / Q000494:pharmacology; D051381:Rats; D013379:Substrate Specificity
D000936:Antigen-Antibody Complex; D003902:Detergents; D004800:Enzymes, Immobilized; D007106:Immune Sera; D011092:Polyethylene Glycols; D017830:Octoxynol; D003066:Coenzyme A Ligases