Abstract
Butyryl-coenzyme A synthetase (butyrate:CoA ligase (AMP-forming), EC 6.2.1.2) from an acetone-dried powder of ox liver mitochondria was found to have a molecular weight of approx. 40 000. The sedimentation equilibrium analysis suggested the presence in solution of higher molecular weight forms of the enzyme and these could also be obtained by extracting the enzyme from the mitochondrial powder in non-reducing conditions. The enzyme was inhibited by sulphydryl reagents, and was found to have at least one available thiol group/molecule. The relationship between enzymic activity and concentration was non-linear, and suggested that an inactive monomer-active dimer equilibrium was present. The 5-6 fold activation by bovine serum albumin required the presence of free thiol groups in the albumin and involved association of albumin with the enzyme. © 1979.
| Original language | English |
|---|---|
| Pages (from-to) | 70-81 |
| Number of pages | 12 |
| Journal | Biochimica et Biophysica Acta (BBA) - Enzymology |
| Volume | 569 |
| Issue number | 1 |
| Publication status | Published - 11 Jul 1979 |
Keywords
- Activation
- Albumin
- Association
- Butyryl-CoA synthetase
- Thiol group