Please use this identifier to cite or link to this item:
|Title:||A method to study kinetics of transnitrosation with nitrosoglutathione: reactions with hemoglobin and other thiols.||Authors:||Rossi, Ranieri
DI SIMPLICIO, P.
|Issue Date:||1997||Project:||None||Journal:||ANALYTICAL BIOCHEMISTRY||Abstract:||
The rate of protein S-nitrosylation, a reversible process by which S-nitroso thiol (RS-NO) compounds exchange the NO+ moiety with protein SH groups, is essentially governed by two factors, the pK alpha and the accessibility of the protein sulfhydryl. A useful method of following transnitrosation kinetics of various protein and nonprotein SH compounds with GS-NO is described. When the reaction is carried out in the presence of 1-chloro-2,4-dinitrobenzene and glutathione transferases, the rate of RS-NO formation (RSH + GS-NO-->RS-NO + GSH) can be monitored by spectrophotometry at 340 nm in terms of the enzymatic conversion of GSH to a GS conjugate. Unlike methods based on NO release from the S-NO bond, this procedure is rapid and accurate and requires relatively small amounts of thiols. The second order rate constants of S-nitrosylation of human and rat oxy- and deoxyhemoglobin of BSA and other thiols were calculated by this method which confirmed previous results reported in the literature
|Appears in Collections:||Publications|
Show full item record
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.