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The human arginases and arginase deficiency
Journal of Inherited Metabolic Disease, 1998AbstractArginase is the final enzyme in the urea cycle. Its deficiency is the least frequently described disorder of this cycle. It results primarily in elevated blood arginine, and less frequently in either persistent or acute elevations in blood ammonia.
R, Iyer +5 more
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Arginase in Glomerulonephritis
Nephron Experimental Nephrology, 2000Arginase metabolizes <i>L</i>-arginine to <i>L</i>-ornithine and urea. Two arginase isoforms, AI (liver arginase) and AII (ubiquitously expressed, functions unknown), have been identified. It is clear that arginases potentially have important roles in addition to urea generation for high concentrations are present at ...
S N, Waddington, V, Cattell
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The Indian Journal of Pediatrics, 1997
Hyperargininemia due to arginase deficiency is a rare, inherited, urea cycle disorder. We report a case of arginase deficiency in a 5-year old boy presenting with mild hyperammonemia, hyperargininemia, and dibasic aminoaciduria.
R, Christopher +2 more
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Hyperargininemia due to arginase deficiency is a rare, inherited, urea cycle disorder. We report a case of arginase deficiency in a 5-year old boy presenting with mild hyperammonemia, hyperargininemia, and dibasic aminoaciduria.
R, Christopher +2 more
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2013
The presence of different sets of several enzymes that participate in the Krebs-Henseleit cycle has been used to identify several genera of trypanosomatids. One of these enzymes is arginase (L-arginine amidinohydrolase, E.C. 3.5.3.1), a metalloenzyme that catalyzes the hydrolysis of L-arginine to L-ornithine and urea.
Maria Fernanda Laranjeira, da Silva +1 more
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The presence of different sets of several enzymes that participate in the Krebs-Henseleit cycle has been used to identify several genera of trypanosomatids. One of these enzymes is arginase (L-arginine amidinohydrolase, E.C. 3.5.3.1), a metalloenzyme that catalyzes the hydrolysis of L-arginine to L-ornithine and urea.
Maria Fernanda Laranjeira, da Silva +1 more
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Liver arginase. III. Properties of highly purified arginase
Archives of Biochemistry and Biophysics, 1956Abstract 1. 1. Arginase has been prepared from horse liver which exhibited one major component and a minor, slower-moving component upon electrophoresis at pH 7.35. Ultracentrifugal analysis also showed the presence of only two components, the lesser of which could be made to sediment as a pellet on the bottom of the cell. This material exhibited
D M, GREENBERG, A E, BAGOT, O A, ROHOLT
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A radiometric assay for arginase
Analytical Biochemistry, 1968Abstract A new radiometric assay for the enzyme arginase has been developed, depending on the conversion of 14 C-guanidoarginine to 14 C-urea and cleavage of the latter to 14 CO 2 by nitrous acid. The advantages of the assay are its accuracy, sensitivity, simplicity, and speed (1.5 hr/assay), compared to existing methods.
P, Righetti, L, De Luca, G, Wolf
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