Regulation of the synthesis and degradation of cytoplasmic 3-hydroxy-3-methylglutaryl coenzyme

Thesis/Dissertation · Wed Dec 31 23:00:00 EST 1986

OSTI ID:6956643

Callaway, K A

3-Hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) synthase was purified to homogeneity from rat liver cytoplasm. The active enzyme is a dimer composed of identical subunits of M/sub r/ = 53,000. Antisera raised to enzyme purified from rats fed a diet containing cholestyramine and mevinolin precipitated HMG-CoA synthase. The antibody precipitated a polypeptide of M/sub r/ = 53,000 after NaDodSO/sub 4/ gel electrophoresis from rat hepatocytes that had been previously incubated with (/sup 35/S) methionine. The rates of synthesis and degradation of HMG-CoA synthase were determined by immunoprecipitation of the enzyme from hepatocytes which were labeled with (/sup 35/S) methionine during pulse and pulse-chase experiments. In hepatocytes isolated from the livers of rats fed either a diet containing cholesterol, a control diet, or a diet containing cholestyramine plus/minus mevinolin, the relative rates of synthase synthesis were 0.12%, 0.20%, 0.30%, and 0.43% respectively, of the rates of total cellular protein synthesis.

• Research Organization: California Univ., Los Angeles (USA)
• OSTI ID: 6956643
• Country of Publication: United States
• Language: English

Related Subjects

550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
AMINO ACIDS
ANIMALS
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
BIOSYNTHESIS
BODY
CARBOXYLIC ACIDS
CELL CONSTITUENTS
CYTOPLASM
DAYS LIVING RADIOISOTOPES
DIGESTIVE SYSTEM
DRUGS
ELECTROPHORESIS
ENZYME IMMUNOASSAY
ENZYMES
EVEN-ODD NUCLEI
FRACTIONATION
GLANDS
IMMUNOASSAY
ISOTOPE APPLICATIONS
ISOTOPES
LIGASES
LIGHT NUCLEI
LIPOTROPIC FACTORS
LIVER
MAMMALS
METABOLISM
METHIONINE
NUCLEI
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC SULFUR COMPOUNDS
ORGANS
RADIOISOTOPES
RATS
RODENTS
SEPARATION PROCESSES
SULFUR 35
SULFUR ISOTOPES
SYNTHESIS
TRACER TECHNIQUES
VERTEBRATES