Substrate specificities of 3-oxoacyl-CoA thiolase a and sterol carrier protein 2/3-oxoacyl-coa thiolase purified from normal rat liver peroxisomes. Sterol carrier protein 2/3-oxoacyl-CoA thiolase is involved in the metabolism of 2-methyl-branched fatty acids and bile acid intermediates

Journal of Biological Chemistry

Volumn 272, Issue 41, 1997, Pages 26023-26031

  Antonenkov, Vasily D ^a,b   Van Veldhoven, Paul P ^a,b   Waelkens, Etienne ^a,c   Mannaerts, Guy P ^a,b  

^a UNIVERSITY OF LEUVEN   (Belgium)

^b Afdeling Farmacologie   (Belgium)

^c Campus Gasthuisberg Univ of Leuven   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

3 OXOACYL ACYL CARRIER PROTEIN SYNTHASE; CARRIER PROTEIN;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME PURIFICATION; FATTY ACID METABOLISM; KINETICS; LIPID PEROXIDATION; NONHUMAN; PEROXISOME; PRIORITY JOURNAL; PROTEIN ANALYSIS; RAT;

ACETYL-COA C-ACETYLTRANSFERASE; ANIMALS; BILE ACIDS AND SALTS; CARRIER PROTEINS; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; FATTY ACIDS; HYDROGEN-ION CONCENTRATION; KINETICS; LIVER; MALE; METHYLATION; MICROBODIES; RATS; RATS, WISTAR; SPECTROPHOTOMETRY, ATOMIC; STEROLS; SUBSTRATE SPECIFICITY;

ANIMALIA;

EID: 0030855998     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.272.41.26023     Document Type: Article

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