Results 161 to 170 of about 65,972 (187)

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

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, Lucile Maria, Floeter-Winter   +1 more
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

Small-molecule Arginase Inhibitors

Pharmaceutical Patent Analyst, 2013
Arginase is an enzyme that metabolizes L-arginine to L-ornithine and urea. In addition to its fundamental role in the hepatic ornithine cycle, it also influences the immune systems in humans and mice. Arginase participates in many inflammatory disorders by decreasing the synthesis of nitric oxide and inducing fibrosis and tissue regeneration.
Yan A, Ivanenkov, Nina V, Chufarova
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, W W, Grody, S D, Cederbaum   +2 more
openaire   +2 more sources

Measurement of arginase activity

Analytical Biochemistry, 1968
Abstract Current methods for determining arginase ( l -arginine amidinohydrolase, EC 3.5.3.1) activity involve the measurement of urea. The carbon dioxide evolved through the action of urease has been measured manometrically (1–3), although more frequently ammonia is determined by established but cumbersome procedures (4, 5).
J J, Hagan, R D, Dallam
openaire   +2 more sources

ARGINASE

Biological Reviews, 1936
SummaryI. Arginase is a highly specific intracellular enzyme and requires that both the carboxyl and the guanidine groups shall be free if the substrate molecule is to be activated. The kinetics of arginase and its behaviour towards activators and inhibitors are very briefly discussed in the text.2.
openaire   +1 more source

Arginases in parasitic diseases

Trends in Parasitology, 2003
Abstract Parasites have elaborated a variety of strategies for invading hosts and escaping immune responses. This article proposes that a common mechanism whereby different parasites escape nitric oxide (NO) toxicity is the activation of arginase. This leads to a depletion of l-arginine (substrate of NO synthase, resulting in lower levels of cytotoxic
Philippe, Vincendeau, Alain P, Gobert, Sylvie, Daulouède, Daniel, Moynet, M Djavad, Mossalayi   +4 more
openaire   +2 more sources

Arginase inhibition

Biochimica et Biophysica Acta (BBA) - Enzymology, 1981
C N, Pace, R A, Landers
openaire   +2 more sources

Arginase

Science, 1941
R, Junowicz-Kocholaty, W, Kocholaty
openaire   +2 more sources