Regulation by oestrogen of carnitine palmitoyltransferase in hepatic mitochondria
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منابع مشابه
Regulation by oestrogen of carnitine palmitoyltransferase in hepatic mitochondria.
Treatment of female rats with ethynyloestradiol decreased both the activity of carnitine palmitoyltransferase and its Ki value for malonyl-CoA compared with pair-fed control rats. In starved rats, carnitine palmitoyltransferase activity and its Ki value for malonyl-CoA were both elevated as expected. Oestrogen treatment had no effect on carnitine palmitoyltransferase activity in the starved sta...
متن کاملCarnitine palmitoyltransferase activities (EC 2.3.1.-) of rat liver mitochondria.
1. A continuously recording and sensitive fluorimetric assay is described for carnitine palmitoyltransferase. This assay has been applied to whole or disintegrated mitochondria and to soluble protein fractions. 2. When rat liver mitochondria had been disintegrated by ultrasound, the specific activity of carnitine palmitoyltransferase was 15-20m-units/mg of protein. Only one-fifth of this activi...
متن کاملEffects of starvation on the carnitine palmitoyltransferase of hepatic peroxisomes.
I t is generally accepted that the mitochondria1 carnitine palmitoyltransferases play an important role in the regulation of hepatic fatty acid oxidation [ I ] . These two enzymes express their activities on either side of the mitochondrial inner membrane that acts as a barrier to the transfer of fatty acids into the mitochondrial matrix. The enzyme that lies outsidc this barrier is located on ...
متن کاملMolecular basis of hepatic carnitine palmitoyltransferase I deficiency.
Mitochondrial fatty acid beta-oxidation is important for energy production, which is stressed by the different defects found in this pathway. Most of the enzyme deficiencies causing these defects are well characterized at both the protein and genomic levels. One exception is carnitine palmitoyltransferase I (CPT I) deficiency, of which until now no mutations have been reported although the defe...
متن کاملIs carnitine palmitoyltransferase inhibited by a malonyl-CoA-binding unit in the mitochondria?
Malonyl-CoA inhibits the carnitine-dependent transport of activated fatty acids into mitochondria by inhibiting the outer carnitine palmitoyltransferase (McGarry et al., 1978). Recent studies in several laboratories have shown that malonyl-CoA is not an ordinary competitive inhibitor of the enzyme. Liver mitochondria from fasted or diabetic rats are less inhibited by malonyl-CoA than are mitoch...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1986
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj2370593