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. | |
PDF
|
|
【 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
【 预 览 】
| Files | Size | Format | View |
|---|---|---|---|
| RO201912020289600ZK.pdf | 180KB |
PDF