نتایج جستجو برای: glycerophosphate

تعداد نتایج: 936  

Journal: :The Journal of biological chemistry 1954
R W SWICK A NAKAO

In 1948, Ogston (1) postulated the existence of an asymmetric enzyme able to distinguish between one of two identical groups in a symmetrical compound. Shortly thereafter, Potter and Heidelberger (2) accomplished the biosynthesis of an “asymmetrically” labeled citric acid, substantiating Ogston’s principle. That glycerol, another compound of chemical symmetry, might also be biologically asymmet...

Journal: :Biochimica et biophysica acta 1988
N Aarsaether R K Berge A Aarsland A Svardal P M Ueland

The effect of methotrexate on lipids in serum and liver and key enzymes involved in esterification and oxidation of long-chain fatty acids were investigated in rats fed a standard diet and a defined choline-deficient diet. Hepatic metabolism of long-chain fatty acids were also studied in rats fed the defined diet with or without choline. When methotrexate was administered to the rats fed the st...

Journal: :Memorias do Instituto Oswaldo Cruz 2000
R P Soares M M Santoro

The alpha-glycerophosphate dehydrogenase (alpha-GPDH) activity in flight muscles of Panstrongylus megistus and Triatoma sordida, vectors of Chagas disease in Brazil, was studied. Both species showed higher enzymatic activities in fliers than in non-fliers insects. T. sordida exhibited a higher proportion of flier insects than P. megistus. A possible role of alpha-GPDH on triatomines flight is d...

Journal: :The Journal of biological chemistry 1994
A Vancura D Haldar

Glycerophosphate acyltransferase (GAT) catalyzes the conversion of sn-glycerol 3-phosphate to lysophosphatidic acid (LPA), the first and committed step of triacylglycerol and phospholipid synthesis. In spite of the important regulatory roles GAT may play in this biosynthetic pathway, little information is available on the structure, biochemical properties, and regulation of GAT from eukaryotic ...

Journal: :Genetics 1973
N Aspinwall

Genetic crosses of alpha-glycerophosphate dehydrogenase (alpha-GPDH) phenotypes in the pink salmon, Oncorhynchus gorbuscha (Walbaum), reveal that this enzyme is encoded by a single locus with two codominant alleles (Slow and Fast). The significance of single gene control of alpha-GPDH is discussed in relation to the purported tetraploid nature of the salmonids.

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