A proportion of rat liver mitochondrial carnitine palmitoyltransferase can be made activatable by malonyl-CoA
| Autor: | David Saggerson, Iraj Ghadiminejad |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
Biophysics
Mitochondria Liver macromolecular substances Cholic Acid Mitochondrion Biochemistry Potassium Chloride chemistry.chemical_compound Enzyme activator Endocrinology PEG ratio medicine Animals Carnitine chemistry.chemical_classification Carnitine O-Palmitoyltransferase Cholic Acids Intracellular Membranes Membrane transport Rats Enzyme Activation Malonyl Coenzyme A enzymes and coenzymes (carbohydrates) Malonyl-CoA Enzyme chemistry lipids (amino acids peptides and proteins) PMSF medicine.drug |
| Zdroj: | Biochimica et biophysica acta. 1085(3) |
| ISSN: | 0006-3002 |
| Popis: | Treatment of rat liver mitochondrial membranes with cholate yields a soluble extract containing carnitine palmitolytransferase (CPT) activity that is insensitive to malonyl-CoA. As found previously ( I. Ghadiminejad and D. Saggerson (1990) FEBS Lett. 269, 406–408 ), addition of polyethylenen glycol 6000 (PEG 6000) to this extract confered sensitivity to malonyl-CoA on the CPT. It is now shown that a sub-population of the CPT activity which is sedimentable at 7000 × g after addition of PEG 6000 is activated by malonyl-CoA, whereas the remainder is inhibited by malonyl-CoA. The presence of KCl increases the proportion of the activatable form of CPT. Possible physiological significance of this finding is discussed. |
| Databáze: | OpenAIRE |
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