Abstract:
:Reduced glutathione is nitrosated in aerobic solutions of nitric oxide under physiological conditions; however, the extent of S-nitrosation was found to be dependent on the inorganic anions present. Of nine anions tested, the bifunctional anions, arsenate, phosphate, and pyrophosphate (40 mM), inhibited the S-nitrosation reaction from 20 to 40%, whereas SO4(2-), H3BO3, SCN-, NO3-, Cl-, and acetate inhibited this reaction < or = 15%. A mechanism of inhibition is presented that involves the catalytic hydrolysis of N2O3 by the bifunctional anions; however, using [18O]phosphate as inhibitor, only 10% of the theoretically produced N2O3 was found to be hydrolyzed to nitrite via this mechanism as calculated from the loss of 18O from phosphate. We conclude that this mechanism accounts for only a minor part of the increased inhibition of S-nitrosation by these bifunctional anions.
journal_name
Biochem Pharmacoljournal_title
Biochemical pharmacologyauthors
DeMaster EG,Quast BJ,Mitchell RAdoi
10.1016/s0006-2952(96)00825-8subject
Has Abstractpub_date
1997-02-21 00:00:00pages
581-5issue
4eissn
0006-2952issn
1873-2968pii
S0006295296008258journal_volume
53pub_type
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pub_type: 杂志文章
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journal_title:Biochemical pharmacology
pub_type: 杂志文章
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journal_title:Biochemical pharmacology
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journal_title:Biochemical pharmacology
pub_type: 杂志文章
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journal_title:Biochemical pharmacology
pub_type: 杂志文章
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journal_title:Biochemical pharmacology
pub_type: 杂志文章
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journal_title:Biochemical pharmacology
pub_type: 杂志文章
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