γ-Radiolysis of Cysteine-Cysteamine Disulfide in Aqueous Solution

1971 ◽  
Vol 49 (5) ◽  
pp. 725-730 ◽  
Author(s):  
J. W. Purdie
Keyword(s):  
Aqueous Solution ◽  
Disulfide Bonds ◽  
Low Oxygen ◽  
Chain Reactions ◽  
Mixed Disulfide ◽  
Deaerated Solution ◽  
A Chain ◽  
Protein Disulfide Bonds ◽  
High Yields ◽  
Protein Disulfide

γ-Radiolysis of a mixed disulfide, cysteine-cysteamine disulfide, in unbuffered aqueous solution (0.3 mM) was investigated in the presence and absence of oxygen. The principal products were the thiols (cysteine and cysteamine), the corresponding sulfinic and sulfonic acids, the symmetrical disulfides (cystine and cystamine) and ammonia. Cystine and cystamine were formed in very high yields in deaerated solution; (G(CySSCy) ~ 15) but addition of oxygen reduced the yield sharply and it was inversely proportional to the oxygen concentration except at very low oxygen levels. In aerated solution G(CySSCy) = 0.8. These observations were attributed to a chain reaction which was suppressed by oxygen:[Formula: see text]In the case of proteins, it was concluded that although chain reactions between RS• radicals and protein disulfide bonds were possible, they should be inhibited by oxygen.

scholarly journals Reduction of protein disulfide bonds in an oxidizing environment

FEBS Letters ◽  
1997 ◽  
Vol 401 (2-3) ◽  
pp. 104-108 ◽  
Author(s):  
Irina Majoul ◽  
David Ferrari ◽  
Hans-Dieter Söling
Keyword(s):  
Disulfide Bonds ◽  
Protein Disulfide Bonds ◽  
Protein Disulfide

Rapid and Sensitive Determination of Protein Disulfide Bonds

Proteins ◽  
1987 ◽  
pp. 493-501 ◽  
Author(s):  
Hsieng S. Lu ◽  
Michael L. Klein ◽  
Richard R. Everett ◽  
Por-Hsiung Lai
Keyword(s):  
Disulfide Bonds ◽  
Sensitive Determination ◽  
Protein Disulfide Bonds ◽  
Protein Disulfide

Protein Disulfide Bonds

2006 ◽  
pp. 1487-1490
Author(s):  
Ervin Welker ◽  
Mahesh Narayan ◽  
Harold A Scheraga
Keyword(s):  
Disulfide Bonds ◽  
Protein Disulfide Bonds ◽  
Protein Disulfide

scholarly journals In-Depth Characterization of Protein Disulfide Bonds by Online Liquid Chromatography-Electrochemistry-Mass Spectrometry

2015 ◽  
Vol 27 (1) ◽  
pp. 50-58 ◽  
Author(s):  
Linda Switzar ◽  
Simone Nicolardi ◽  
Julie W. Rutten ◽  
Saskia A. J. Lesnik Oberstein ◽  
Annemieke Aartsma-Rus ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Liquid Chromatography ◽  
Disulfide Bonds ◽  
Protein Disulfide Bonds ◽  
Protein Disulfide

Radiation-induced oxidation of 2-propanol by hydrogen peroxide in aqueous solutions

1970 ◽  
Vol 48 (8) ◽  
pp. 1232-1238 ◽  
Author(s):  
C. E. Burchill ◽  
I. S. Ginns
Keyword(s):  
Aqueous Solution ◽  
Hydrogen Peroxide ◽  
Aqueous Solutions ◽  
Lower Limit ◽  
Alcohol Concentration ◽  
Chain Mechanism ◽  
Radiation Induced ◽  
A Chain ◽  
High Yields ◽  
Radical Conversion

The radiation-induced oxidation of 2-propanol by hydrogen peroxide in neutral deaerated aqueous solution has been investigated. 2-Propanol is oxidized to acetone, and hydrogen peroxide reduced in stoichiometrically equivalent high yields. The yields are independent of hydrogen peroxide concentration in the range 5 × 10−2 to 10−3 M and linearly dependent on alcohol concentration in the range 0.13 to 1.05 M. The reaction yields increased with decreasing dose rate.The results are explained by a chain mechanism in which initiation occurs via H-atom abstraction from 2-propanol to form either (CH3)2ĊOH (1) or CH3 CHOH ĊH2 (2). 1 reacts with H2O2 in a chain propagating reaction[Formula: see text]2 may abstract the α hydrogen from the parent alcohol[Formula: see text]or undergo bimolecular termination. A lower limit of 53 ± 101mole−1 s−1 is estimated for the rate constant for this radical conversion reaction.

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