Peroxisome Proliferative Drugs Do not Induce an Increase of Rat Mevalonate Pyrophosphate Decarboxylase.

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Peroxisome proliferative drugs do not induce an increase of rat mevalonate pyrophosphate decarboxylase.

To determine whether or not the expression of mevalonate pyrophosphate decarboxylase (MPD) depends on the proliferation of peroxisomes, we examined change in the protein level of MPD in the crude extract, the cytosol and the peroxisome-enriched fraction of the livers of rats administered peroxisome proliferative drugs. No increase of MPD was observed in any of these fractions. These data sugges...

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Subcellular distribution of mouse mevalonate pyrophosphate decarboxylase.

Mevalonate pyrophosphate decarboxylase (MPD) is considered to be a cytosolic protein. Recently, other groups reported that MPD is mostly located in the peroxisomes. In this study, we examined whether the expression of MPD in mice depends on the proliferation of peroxisomes, and whether MPD is predominantly located in the peroxisomes or the cytosol of mice. No increase in the protein level of MP...

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Inhibition of rat liver mevalonate pyrophosphate decarboxylase and mevalonate phosphate kinase by phenyl and phenolic compounds.

1. Mevalonate pyrophosphate decarboxylase of rat liver is inhibited by various phenyl and phenolic acids. 2. Some of the phenyl and phenolic acids also inhibited mevalonate phosphate kinase. 3. Compounds with the phenyl-vinyl structure were more effective. 4. Kinetic studies showed that some of the phenolic acids compete with the substrates, mevalonate 5-phosphate and mevalonate 5-pyrophosphate...

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Purification and characterization of mouse mevalonate pyrophosphate decarboxylase.

Mevalonate pyrophosphate decarboxylase (MPD) in mouse liver was purified by affinity chromatography. The purified enzyme was a homodimer of 46-kDa subunits and had an isoelectric point of 5.0. Kinetic analysis revealed an apparent Km value of 10 microm for mevalonate pyrophosphate. The enzyme required ATP as a phosphate acceptor and Mg as a divalent cation, which could be substituted with Mn or...

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Mevalonate pyrophosphate decarboxylase is predominantly located in the cytosol of rat hepatocytes.

Mevalonate pyrophosphate decarboxylase (MPD) is found in the 100000 x g supernatant fraction of cells or tissues and is considered to be a cytosolic protein. Recently, other groups reported that MPD is mostly located in the peroxisomes. In this study, we used two different methods to determine whether MPD is predominantly located in the peroxisomes or the cytosol of rat hepatocytes. 1) In perme...

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ژورنال

عنوان ژورنال: Biological and Pharmaceutical Bulletin

سال: 2003

ISSN: 0918-6158,1347-5215

DOI: 10.1248/bpb.26.93