Results 251 to 260 of about 50,915 (302)
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Arginase in Leishmania

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
openaire   +2 more sources

Arginase Promotes Neointima Formation in Rat Injured Carotid Arteries

open access: yesArteriosclerosis, Thrombosis, and Vascular Biology, 2009
Objective—Arginase stimulates the proliferation of cultured vascular smooth muscle cells (VSMCs); however, the influence of arginase on VSMC growth in vivo is not known.
William Durante   +2 more
exaly   +2 more sources

Liver arginase. III. Properties of highly purified arginase

Archives of Biochemistry and Biophysics, 1956
Abstract 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
openaire   +2 more sources

Comparative properties of arginases

Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 1996
Arginase is a primordial enzyme, widely distributed in the biosphere and represented in all primary kingdoms. It plays a critical role in the hepatic metabolism of most higher organisms as a cardinal component of the urea cycle. Additionally, it occurs in numerous organisms and tissues where there is no functioning urea cycle. Many extrahepatic tissues
C P, Jenkinson   +2 more
openaire   +2 more sources

A radiometric assay for arginase

Analytical Biochemistry, 1968
Abstract 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
openaire   +2 more sources

Purification of arginase

Experientia, 1948
Nombreux sont les travaux qui traitent de la separation et de la purification de l'arginase. Le present travail decrit une methode de purification qui permet d'obtenir une arginase active contenant des traces d'impuretes (80% d'arginase active).
openaire   +2 more sources

Arginase-1 deficiency

Journal of Molecular Medicine, 2015
Arginase-1 (ARG1) deficiency is a rare autosomal recessive disorder that affects the liver-based urea cycle, leading to impaired ureagenesis. This genetic disorder is caused by 40+ mutations found fairly uniformly spread throughout the ARG1 gene, resulting in partial or complete loss of enzyme function, which catalyzes the hydrolysis of arginine to ...
Yuan Yan, Sin   +3 more
openaire   +2 more sources

Arginase

British Journal of Pharmacology, 2009
Allergic asthma is a chronic inflammatory airways' disease, characterized by allergen-induced early and late bronchial obstructive reactions, airway hyperresponsiveness (AHR), airway inflammation and airway remodelling. Recent ex vivo and in vivo studies in animal models and asthmatic patients have indicated that arginase may play a central role in all
Maarsingh, Harm   +2 more
openaire   +1 more source

Assay and kinetics of arginase

Analytical Biochemistry, 1986
A sensitive colorimetric assay for arginase was developed. Urea produced by arginase was hydrolyzed to ammonia by urease, the ammonia was converted to indophenol, and the absorbance was measured at 570 nm. The assay is useful with low concentrations of arginase (0.5 munit or less than 1 ng rat liver arginase) and with a wide range of arginine ...
C L, Garganta, J S, Bond
openaire   +2 more sources

Human platelet arginase

Molecular and Cellular Biochemistry, 1980
We report here, for the first time the presence of arginase in human platelets. This enzyme has been partially purified and some of it properties studied. Its biological significance and its involvement in polyamine biosynthesis are considered.
V R, Villanueva, M, Giret
openaire   +2 more sources

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