Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/4238
Title: A method to study kinetics of transnitrosation with nitrosoglutathione: reactions with hemoglobin and other thiols.
Authors: Rossi, Ranieri 
Lusini, L.
Giannerini, F.
Giustarini, Daniela 
Lungarella, Giuseppe
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
Description: 
18323
URI: http://hdl.handle.net/20.500.12779/4238
ISSN: 0003-2697
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