The acyl-CoAamino acid N-acyltransferases were partially purified from human liver mitochondria. The aralkyl transferase (ArAlk) had glycine conjugating activity toward the fol- Its kinetic properties and responses to salt were very similar to those of bovine ArAlk. Further, its molecular weight wa
Characterization of acyl-CoA:Cholesterol acyltransferase from neonatal chick liver
โ Scribed by C. Marco; L.G. Morillas; J.L. Segovia; E. Garcia-Phreurin
- Publisher
- Elsevier Science
- Year
- 1986
- Tongue
- English
- Weight
- 618 KB
- Volume
- 18
- Category
- Article
- ISSN
- 0020-711X
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When bovine kidney mitochondria were assayed in the presence of Triton X-100, they were found to contain glycine N-acyltransferase activity toward the CoA-adducts of benzoate, butyrate, isovalerate, naphthylacetate, phenylacetate, and salicylate. Heptanoyl-CoA activity was masked by high acyl-CoA hy
The arylacetyl acyl-CoA:amino acid N-acyltransferase was previously purified to homogeneity from bovine liver mitochondria, and partial sequences were obtained for peptides generated by cyanogen bromide cleavage of the enzyme. One of these sequences was used to design an oligonucleotide probe that w