𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Purification to Homogeneity of Mitochondrial Acyl CoA: Glycine N-Acyltransferase from Human Liver

✍ Scribed by Y.R. Mawal; I.A. Qureshi

Book ID
115575842
Publisher
Elsevier Science
Year
1994
Tongue
English
Weight
392 KB
Volume
205
Category
Article
ISSN
0006-291X

No coin nor oath required. For personal study only.

πŸ“œ SIMILAR VOLUMES

Isolation and characterization of mitoch
Isolation and characterization of mitochondrial acyl-coa: Glycine n-acyltransferases from kidney
✍ Kelley, Michael ;Vessey, Donald A. πŸ“‚ Article πŸ“… 1993 πŸ› John Wiley and Sons 🌐 English βš– 701 KB

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

Characterization of the acyl-CoA: Amino
Characterization of the acyl-CoA: Amino acid N-acyltransferases from primate liver mitochondria
✍ Kelley, Michael ;Vessey, Donald A. πŸ“‚ Article πŸ“… 1994 πŸ› John Wiley and Sons 🌐 English βš– 588 KB

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