-transparent.png){kind=logo}
1. Rhodanese inactivation by 2,4,6-trinitrobenzenesulphonate, in the presence of n-butylamine in the reaction medium, has been studied by a kinetic analysis of the data, based on the assumption that enzyme inactivation is brought about by direct reaction of this with the modifying agent. 2. Initial reaction rates for rhodanese activity loss were determined by a mathematical analysis of the first three recorded values of rhodanese residual activity. 3. It was found that fractional rhodanese activity values, at infinite reaction time with 2,4,6-trinitrobenzenesulphonate (end-point values), were significantly lower than the values calculated on the assumption of rhodanese inactivation being entirely due to direct trinitrophenylation of enzyme protein. 4. Also, initial enzyme inactivation values were higher in the presence, rather than in the absence, of n-butylamine. 5. These results indicate that 2,4,6-trinitrobenzenesulphonate-induced rhodanese inactivation, in the presence of n-butylamine in the reaction medium, is due to the generation of a highly reactive, unstable intermediate, probably a free radical species.
E T Rakitzis, and
T B Malliopoulou
April 1990,
The Journal of biological chemistry,
E T Rakitzis, and
T B Malliopoulou
March 2000,
FEBS letters,
E T Rakitzis, and
T B Malliopoulou
December 1947,
Nature,
E T Rakitzis, and
T B Malliopoulou
February 1977,
Proceedings of the National Academy of Sciences of the United States of America,
E T Rakitzis, and
T B Malliopoulou
June 2013,
European journal of inorganic chemistry,
E T Rakitzis, and
T B Malliopoulou
April 1967,
Biochemistry,
E T Rakitzis, and
T B Malliopoulou
November 1966,
The Journal of biological chemistry,
E T Rakitzis, and
T B Malliopoulou
May 1967,
The Journal of biological chemistry,
E T Rakitzis, and
T B Malliopoulou
November 1978,
Biochemistry,
E T Rakitzis, and
T B Malliopoulou
July 1976,
Biochimica et biophysica acta,
