Properties of 3 hydroxy 3 methylglutaryl coenzyme A reductase solubilized from rat liver and hepatoma

M. S. Brown, S. E. Dana, M. D. Siperstein

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

In hepatomas, the activity of 3 hydroxy 3 methylglutaryl coenzyme A reductase, the rate controlling enzyme in cholesterol biosynthesis, is not normally suppressed by cholesterol. To examine the biochemical mechanism of this loss of feedback control of cholesterol synthesis, a comparison was made of the properties of 3 hydroxy 3 methylglutaryl coenzyme A reductase after solubilization and partial purification from microsomes of normal rat liver and of a minimal deviation rat hepatoma. The solubilized enzyme from the 2 sources behaved identically with respect to substrate kinetics, heat inactivation, and inactivation, and gel filtration. By the use of a new method that permits assay of 3 hydroxy 3 methylglutaryl coenzyme A reductase activity after polyacrylamide gel electrophoresis, it was shown that the solubilized hepatoma enzyme and the normal liver enzyme had similar electrophoretic mobility. It is concluded that the failure of hepatomas to suppress 3 hydroxy 3 methylglutaryl coenzyme A reductase activity is not due to the production of an altered form of the enzyme. (27 references.)

Original languageEnglish (US)
Pages (from-to)6585-6589
Number of pages5
JournalJournal of Biological Chemistry
Volume249
Issue number20
StatePublished - 1974

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Liver
Rats
Hepatocellular Carcinoma
Oxidoreductases
Enzymes
Cholesterol
Electrophoretic mobility
Biosynthesis
Microsomes
Electrophoresis
Feedback control
Purification
Gel Chromatography
Polyacrylamide Gel Electrophoresis
Assays
Hot Temperature
Gels
3-hydroxy-3-methylglutaryl-coenzyme A
Kinetics
Substrates

ASJC Scopus subject areas

  • Biochemistry

Cite this

Properties of 3 hydroxy 3 methylglutaryl coenzyme A reductase solubilized from rat liver and hepatoma. / Brown, M. S.; Dana, S. E.; Siperstein, M. D.

In: Journal of Biological Chemistry, Vol. 249, No. 20, 1974, p. 6585-6589.

Research output: Contribution to journalArticle

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