Phospholipid requirement for 2-acetamidofluorene N-and ring-hydroxylation by hamster liver microsomal cytochrome P-450 enzyme system. 1977

P D Lotlikar, and E N Dwyer, and W J Baldy, and J Nyce

A phospholipid requirement of 2-acetamidofluorene N- and ring-hydroxylation was investigated with partially delipidated microsomal fraction from livers of 3-methylcholanthrene-pretreated hamsters. Butan-1-ol extraction of microsomal fraction removed 90% of the total lipid content without any appreciable effect on microsomal proteins. Such extracted microsomal fractions had much lower capacity to N- and ring-hydroxylate 2-acetamidofluorene: 25 and 44% of control respectively. Addition of butan-1-ol-extracted total lipid restored both oxidations to some extent, whereas addition of phosphatidylcholine fraction restored both oxidations almost completely. Addition of synthetic phospholipid, dilauroyl phosphatidylcholine, restored both oxidations to a large extent, whereas synthetic dipalmitoyl or distearoyl phosphatidylcholine was ineffective in restoring these oxidations.

UI MeSH Term Description Entries
D008748 Methylcholanthrene A carcinogen that is often used in experimental cancer studies. 20-Methylcholanthrene,3-Methylcholanthrene,20 Methylcholanthrene,3 Methylcholanthrene
D008862 Microsomes, Liver Closed vesicles of fragmented endoplasmic reticulum created when liver cells or tissue are disrupted by homogenization. They may be smooth or rough. Liver Microsomes,Liver Microsome,Microsome, Liver
D010743 Phospholipids Lipids containing one or more phosphate groups, particularly those derived from either glycerol (phosphoglycerides see GLYCEROPHOSPHOLIPIDS) or sphingosine (SPHINGOLIPIDS). They are polar lipids that are of great importance for the structure and function of cell membranes and are the most abundant of membrane lipids, although not stored in large amounts in the system. Phosphatides,Phospholipid
D003577 Cytochrome P-450 Enzyme System A superfamily of hundreds of closely related HEMEPROTEINS found throughout the phylogenetic spectrum, from animals, plants, fungi, to bacteria. They include numerous complex monooxygenases (MIXED FUNCTION OXYGENASES). In animals, these P-450 enzymes serve two major functions: (1) biosynthesis of steroids, fatty acids, and bile acids; (2) metabolism of endogenous and a wide variety of exogenous substrates, such as toxins and drugs (BIOTRANSFORMATION). They are classified, according to their sequence similarities rather than functions, into CYP gene families (>40% homology) and subfamilies (>59% homology). For example, enzymes from the CYP1, CYP2, and CYP3 gene families are responsible for most drug metabolism. Cytochrome P-450,Cytochrome P-450 Enzyme,Cytochrome P-450-Dependent Monooxygenase,P-450 Enzyme,P450 Enzyme,CYP450 Family,CYP450 Superfamily,Cytochrome P-450 Enzymes,Cytochrome P-450 Families,Cytochrome P-450 Monooxygenase,Cytochrome P-450 Oxygenase,Cytochrome P-450 Superfamily,Cytochrome P450,Cytochrome P450 Superfamily,Cytochrome p450 Families,P-450 Enzymes,P450 Enzymes,Cytochrome P 450,Cytochrome P 450 Dependent Monooxygenase,Cytochrome P 450 Enzyme,Cytochrome P 450 Enzyme System,Cytochrome P 450 Enzymes,Cytochrome P 450 Families,Cytochrome P 450 Monooxygenase,Cytochrome P 450 Oxygenase,Cytochrome P 450 Superfamily,Enzyme, Cytochrome P-450,Enzyme, P-450,Enzyme, P450,Enzymes, Cytochrome P-450,Enzymes, P-450,Enzymes, P450,Monooxygenase, Cytochrome P-450,Monooxygenase, Cytochrome P-450-Dependent,P 450 Enzyme,P 450 Enzymes,P-450 Enzyme, Cytochrome,P-450 Enzymes, Cytochrome,Superfamily, CYP450,Superfamily, Cytochrome P-450,Superfamily, Cytochrome P450
D005449 Fluorenes A family of diphenylenemethane derivatives.
D006224 Cricetinae A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS. Cricetus,Hamsters,Hamster
D006900 Hydroxylation Placing of a hydroxyl group on a compound in a position where one did not exist before. (Stedman, 26th ed) Hydroxylations
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D015073 2-Acetylaminofluorene A hepatic carcinogen whose mechanism of activation involves N-hydroxylation to the aryl hydroxamic acid followed by enzymatic sulfonation to sulfoxyfluorenylacetamide. It is used to study the carcinogenicity and mutagenicity of aromatic amines. 2-Acetamidofluorene,Fluoren-2-ylacetamide,2-AAF,2-Fluorenylacetamide,AAF, Aminofluorene,Acetylaminofluorene,N-2-Fluorenylacetamide,N-Acetyl-2-Aminofluorene,2 Acetamidofluorene,2 Acetylaminofluorene,2 Fluorenylacetamide,Aminofluorene AAF,Fluoren 2 ylacetamide,N 2 Fluorenylacetamide,N Acetyl 2 Aminofluorene
D066298 In Vitro Techniques Methods to study reactions or processes taking place in an artificial environment outside the living organism. In Vitro Test,In Vitro Testing,In Vitro Tests,In Vitro as Topic,In Vitro,In Vitro Technique,In Vitro Testings,Technique, In Vitro,Techniques, In Vitro,Test, In Vitro,Testing, In Vitro,Testings, In Vitro,Tests, In Vitro,Vitro Testing, In

Related Publications

P D Lotlikar, and E N Dwyer, and W J Baldy, and J Nyce
September 1975, The Biochemical journal,
P D Lotlikar, and E N Dwyer, and W J Baldy, and J Nyce
April 1982, Toxicology letters,
P D Lotlikar, and E N Dwyer, and W J Baldy, and J Nyce
January 1975, Biochemical pharmacology,
P D Lotlikar, and E N Dwyer, and W J Baldy, and J Nyce
May 1980, The Journal of biological chemistry,
P D Lotlikar, and E N Dwyer, and W J Baldy, and J Nyce
January 1991, Chemical research in toxicology,
P D Lotlikar, and E N Dwyer, and W J Baldy, and J Nyce
August 1974, Biochemical and biophysical research communications,
P D Lotlikar, and E N Dwyer, and W J Baldy, and J Nyce
November 1974, The Biochemical journal,
P D Lotlikar, and E N Dwyer, and W J Baldy, and J Nyce
May 1987, Archives of biochemistry and biophysics,
P D Lotlikar, and E N Dwyer, and W J Baldy, and J Nyce
December 1973, The Biochemical journal,
P D Lotlikar, and E N Dwyer, and W J Baldy, and J Nyce
September 1981, Biochemical and biophysical research communications,
Copied contents to your clipboard!