期刊论文详细信息
FEBS Letters
Transacylase activity of lactating bovine mammary fatty acid synthase
Kumar, Soma1  Anderson, Gregory J.1 
[1] Department of Chemistry, Georgetown University, Washington, DC 20057, USA
关键词: Transacylase;    Fatty acid synthase;    Acyl exchange;    Substrate specificity;   
DOI  :  10.1016/0014-5793(87)80839-6
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

An assay for the transacylation reaction catalyzed by fatty acid synthase was developed which does not require model substrates or labelled acyl-derivatives of CoA. It involves the transfer of the acyl group from unlabelled CoA to [3H]CoA. This assay shows the occurrence of transacylation at a relatively high rate with a variety of substrates that the enzyme is able to utilize. The activity is unaffected by dissociation of the enzyme or modification by iodoacetamide or 2-chloroacetyl-CoA.

【 授权许可】

Unknown   

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