Results 231 to 240 of about 78,666 (255)
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Measurement of arginase activity
Analytical Biochemistry, 1968Abstract 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
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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.
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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.
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Arginases in parasitic diseases
Trends in Parasitology, 2003Abstract 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 +4 more
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Rejuvenation Research, 2019
Reduced bioavailability of nitric oxide (NO) is accompanied by endothelial dysfunction, which precedes clinical signs of atherosclerosis. The metalloenzyme arginase reciprocally inhibits the formation of NO and available data demonstrate that arginase ...
A. Mahdi, J. Pernow, Oskar Kövamees
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Reduced bioavailability of nitric oxide (NO) is accompanied by endothelial dysfunction, which precedes clinical signs of atherosclerosis. The metalloenzyme arginase reciprocally inhibits the formation of NO and available data demonstrate that arginase ...
A. Mahdi, J. Pernow, Oskar Kövamees
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Biochimica et Biophysica Acta (BBA) - Enzymology, 1981
C N, Pace, R A, Landers
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C N, Pace, R A, Landers
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Arginase and its mechanisms in Leishmania persistence
Parasite immunology (Print), 2020Gabriela Pessenda, J. Santana da Silva
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2020
The present invention relates to novel arginase inhibitors of formula (I). These novel compounds are useful in the treatment of diseases that are associated with arginase activity, such as asthma, allergic rhinitis and COPD (chronic obstructive pulmonary disease).
Kurhade, Santosh, Dömling, Alexander
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The present invention relates to novel arginase inhibitors of formula (I). These novel compounds are useful in the treatment of diseases that are associated with arginase activity, such as asthma, allergic rhinitis and COPD (chronic obstructive pulmonary disease).
Kurhade, Santosh, Dömling, Alexander
openaire