from The American Heritage® Dictionary of the English Language, 4th Edition
- n. An enzyme found primarily in the liver that catalyzes the hydrolysis of arginine to form urea and ornithine.
from Wiktionary, Creative Commons Attribution/Share-Alike License
- n. An enzyme that catalyses the hydrolysis of arginine to form urea and ornithine
from The Century Dictionary and Cyclopedia
- n. A ferment which causes the decomposition of arginin into ornithin and urea. It has been found in the liver, the thymus, lymph glands, the mucosa of the small intestine, etc.
Aminoacidopathies (maple syrup urine disease; homocystinuria; cobalamin deficiencies; tyrosinemia; urea cycle defects (ornithine transcarbamylase, carbamyl phosphate synthase, citrullinemia, argininosuccinic aciduria, arginase deficiencies) and non-ketotic hyperglycinemia)
D. Dakin he investigated arginase, the ferment which hydrolyses arginine into urea and ornithine, and later he discovered agmatine in herring roe and devised a method for preparing it.
In the periphery, the NO production decrease may reflect an arginase-mediated synthesis of polyamines necessary to trypanosome growth.
Elevated levels of the enzyme arginase contribute to vascular eye damage and Medical College of Geor ...
To test whether the predominance of the arginase expression over that of the iNOS endowed M2 MØ with reparative capabilities, vascular smooth muscle cells (VSMCs) were cultured with MØ-conditioned medium.
Jenkinson CP, Griscavage JM, Kern RM, Arabolos NS, et al. (1995) Co-induction of arginase and nitric oxide synthase in murine macrophages activated by lipopolysaccharide.
Eichmann K, Modolell M (1998) Alternative metabolic states in murine macrophages reflected by the nitric oxide synthase/arginase balance: competitive regulation by CD4+ T cells correlates with Th1/Th2 phenotype.
El Kasmi KC, Qualls JE, Pesce JT, Smith AM, Thompson RW, et al. (2008) Toll-like receptor-induced arginase 1 in macrophages thwarts effective immunity against intracellular pathogens.
B: Primary aortic vascular smooth muscle cells (VSMCs) from C57Bl/6 mice were cultured for 48 hours in the presence of media conditioned by C57Bl/6 M1 or M2 MØ which were polarized in the presence of the PPARγ agonist pioglitazone (Pio), the PPARγ antagonist GW9662 (GW), or the arginase inhibitor Nor-NOHA.
In the present study, we used Arg I and Arg II as surrogate markers of M1 and M2 MØ since these two isoforms of arginase were distinctly upregulated in bone marrow-derived M1 and M2 MØ polarized in vitro.
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