نتایج جستجو برای: malonyl dichloride

تعداد نتایج: 3527  

Journal: :The Biochemical journal 1994
R L Mynatt J J Greenhaw G A Cook

It has been reported that sodium cholate can separate the catalytic component of carnitine palmitoyltransferase-I (CPT-I) from a putative malonyl-CoA-binding regulatory protein capable of conferring sensitivity to malonyl-CoA on CPT-II. We found that cholate preferentially extracted a contaminating malonyl-CoA-sensitive CPT from mitochondrial inner membranes. When cholate extracts of outer memb...

Journal: :The Biochemical journal 1995
N M Broadway E D Saggerson

Conditions have been developed for the solubilization of hepatic microsomal carnitine acyltransferase activity in good yield, with excellent long-term stability and with retention of malonyl-CoA sensitivity. Solubilized microsomal carnitine acyltransferase activity can be separated into malonyl-CoA-sensitive and -insensitive activities either by gel filtration on Superdex 200 or by anion-exchan...

Journal: :Food chemistry 2015
Michael Vagiri Sean Conner Derek Stewart Staffan C Andersson Susan Verrall Eva Johansson Kimmo Rumpunen

Blackcurrant leaves are an essential source of phenolic compounds and this study investigated their variation relative to leaf positions and harvest date. The phenolic content varied between harvest dates, although leaf position on the shoot and interactions also played an important role. The contents of quercetin-malonyl-glucoside, kaempferol-malonyl-glucoside isomer and kaempferol-malonyl-glu...

Journal: :The Biochemical journal 1997
N M Broadway E D Saggerson

We have investigated the extent to which membrane environment affects the catalytic properties of the malonyl-CoA-sensitive carnitine acyltransferase of liver microsomal membranes. Arrhenius-type plots of activity were linear in the absence and presence of malonyl-CoA (2.5 microM). Sensitivity to malonyl-CoA increased with decreasing assay temperature. Partly purified enzyme displayed an increa...

2010
Francis P. Kuhajda

F atty a cid s ynthase ( FAS) inhibition initiates selective ap optosis o f can cer cel ls b oth in vivo and in vitro, which m ay i nvolve malonyl-CoA metabolism. T hese findings l ed to exploration of malonyl-CoA decarboxylase ( MCD) as a p otential novel target for cancer treatment. M CD regulates the levels of cellular malonyl-CoA through the decarboxylation of malonyl-CoA to acetyl-CoA. Mal...

2005
David SAGGERSON

1. [14C]Malonyl-CoA bound to intact mitochondria isolated from rat liver and heart in a manner consistent with the presence of two independent classes of binding sites in each tissue. 2. The binding characteristics for mitochondria obtained from fed male rats were: for heart, KD(1) = 1 -l8 nM, KD(2) = 30uM, N1 = 7pmol/mg of protein, N2 = approx. 660pmol/mg of protein; for liver, KD(1) = 0.1 M, ...

2017
VALENTINA N. GLUSHkO

Study of interaction between catechol and tetraethylene glycol dichloride in the n-butanol media, resulting with benzo-15-crown-5 production. Production of nitroand amino-derivatives of benzo-15-crown-5. Determination of their thermogravimetric characteristics. keywords: benzo-15-crown-5, catechol, tetraethylene glycol dichloride, crown ether, gas liquid chromatography, chromate-mass spectrometry

Journal: :The Journal of biological chemistry 1978
G A Cook M T King R L Veech

We have measured rates of ketogenesis and malonyl-CoA contents of hepatocytes isolated from meal-fed rats under a variety of incubation conditions in order to determine the relationship between the intracellular malonyl-CoA level and the rate of ketogenesis. Evidence obtained from rat liver homogenates suggested that malonyl-CoA, which is a major determinant of fatty acid synthesis in vivo, als...

Journal: :The Journal of biological chemistry 1979
S R Keyes J A Alfano I Jansson D L Cinti

Participation of cytochrome b5 in the liver microsomal elongation of fatty acids in the rat is suggested by (a) an increase in the rate of reoxidation of liver microsomal cytochrome b5, following reduction by NADH, in the presence of both malonyl coenzyme A and ATP, and (b) a 60% inhibition of incorporation of malonyl-CoA into microsomal fatty acids in the presence of anti-cytochrome b6 IgG; co...

Journal: :American journal of physiology. Endocrinology and metabolism 2000
D Chien D Dean A K Saha J P Flatt N B Ruderman

Malonyl-CoA acutely regulates fatty acid oxidation in liver in vivo by inhibiting carnitine palmitoyltransferase. Thus rapid increases in the concentration of malonyl-CoA, accompanied by decreases in long-chain fatty acyl carnitine (LCFA-carnitine) and fatty acid oxidation have been observed in liver of fasted-refed rats. It is less clear that it plays a similar role in skeletal muscle. To exam...

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