## Abstract Shortβ, mediumβ, and longβchain fatty acid:CoA ligases from human liver were tested for their sensitivity to inhibition by triacsin C. The shortβchain fatty acid:CoA ligase was inhibited less than 10% by concentrations of triacsin C as high as 80 ΞΌM. The two mitochondrial xenobiotic/med
Characterization of the CoA ligases of human liver mitochondria catalyzing the activation of short- and medium-chain fatty acids and xenobiotic carboxylic acids
β Scribed by Donald A. Vessey; Michael Kelley; Robert S. Warren
- Book ID
- 117481886
- Publisher
- Elsevier Science
- Year
- 1999
- Tongue
- English
- Weight
- 186 KB
- Volume
- 1428
- Category
- Article
- ISSN
- 0304-4165
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A radiolabeled ATP assay was developed for measuring carboxylic acid:CoA ligase activity. The assay was designed to measure the formation of [gamma-33P]pyrophosphate from [gamma-33P]ATP in the course of the reaction. The assay was linear with protein concentration, and rates as low as 1 pmol/min wer
A mitochondria1 freezetthaw lysate was fractionated on a DEAE-cellulose column into four distinct acyl-CoA ligase fractions. First to elute was a 50 kDa short-chain ligase that activated only short-chain fatty acids. Next to elute were three ligases that had activity toward both medium-chain fatty a
## Abstract The purification of xenobiotic/mediumβchain fatty acid:CoA ligases (XMβligases) from human liver mitochondria resulted in the isolation of two chromatographically separable forms (HXMβA and HXMβB). These two forms were purified to near homogeneity, cleaved with cyanogen bromide, the res