Soeda S, Kishimoto Y, Hashimoto T
Biochem Int. 1986 Feb;12(2):225-33.
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.
从大鼠肝脏微粒体中纯化得到的脂肪酰辅酶A合成酶被固定在溴化氰活化的琼脂糖4B或活化的CH-琼脂糖4B上，并对其从二十四烷酸（C24:0）和棕榈酸（C16:0）合成辅酶A酯的酶活性进行了研究和比较。用CH-琼脂糖时，二十四烷酰辅酶A与棕榈酰辅酶A的合成活性比增加了4.5倍，而用溴化氰琼脂糖时仅略有增加。去污剂和离液剂对两种底物的影响因固定化而显著改变。因此，本研究结果表明，脂肪酰辅酶A合成酶的稳定性和脂肪酸特异性受酶的物理状态显著影响。
