Source:http://linkedlifedata.com/resource/pubmed/id/11897356
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3-4
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pubmed:dateCreated |
2002-3-18
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pubmed:abstractText |
The inhibitory effects of anions, such as N(3)(-), NO(2)(-), BO(4)(3-), SCN(-), CH(3)COO(-), SO(4)(2-), ClO(4)(-), H(2)PO(4)(-), CN(-), I(-), Br(-), Cl(-) and F(-), on the hydrolysis of L-arginine (L-Arg) by rat liver arginase (RLA) have been studied. From all these anions, only F(-) exhibited a clear inhibitory effect at the mM level. Inhibition of RLA by F(-) is reversible and uncompetitive towards L-Arg binding with a K(i) value of 1.3+/-0.5 mM at pH 7.4. This effect is dependent on pH as the IC(50) value of F(-) towards RLA increases from 1.2 to 19 mM when increasing the pH from 7 to 10. Another specific inhibitor of RLA, N(omega)-hydroxy-L-nor-arginine (nor-NOHA), that has been recently shown to bind to RLA as a bridging ligand of its (Mn(II))(2) cluster, exhibits some similarities with F(-) in its inhibitory effects (identical pH dependence). It is thus tempting to propose that the inhibitory effects of F(-) could be due to its binding as a bridging ligand of the RLA (Mn(II))(2) cluster. However, further studies are required to determine the modes of interaction of F(-) with RLA.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Anions,
http://linkedlifedata.com/resource/pubmed/chemical/Arginase,
http://linkedlifedata.com/resource/pubmed/chemical/Arginine,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Fluorides
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0162-0134
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
88
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
397-402
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11897356-Animals,
pubmed-meshheading:11897356-Anions,
pubmed-meshheading:11897356-Arginase,
pubmed-meshheading:11897356-Arginine,
pubmed-meshheading:11897356-Enzyme Inhibitors,
pubmed-meshheading:11897356-Fluorides,
pubmed-meshheading:11897356-Hydrogen-Ion Concentration,
pubmed-meshheading:11897356-Liver,
pubmed-meshheading:11897356-Male,
pubmed-meshheading:11897356-Models, Molecular,
pubmed-meshheading:11897356-Rats,
pubmed-meshheading:11897356-Rats, Sprague-Dawley
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pubmed:year |
2002
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pubmed:articleTitle |
Interaction of anions with rat liver arginase: specific inhibitory effects of fluoride.
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pubmed:affiliation |
Laboratoire de Chimie et Biochimie Pharmacologiques et Toxicologiques, UMR 8601, Université René Descartes, 45 Rue des Saints-Pères, 75270 Paris Cedex 06, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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