1. The inactivation of rat skeletal muscle AMP deaminase by Dnp-F (1-fluoro-2,4-dinitrobenzene) is accompanied by the arylation of thiol, amino and phenolic hydroxyl groups. 2. The number of thiol groups that react with Dnp-F is about 12; this is the number that reacts with Nbs2 [5,5′-dithiobis-(2-nitrobenzoic acid)] and N-ethylmaleimide without loss of enzyme activity, and it appears to be the same thiol groups that all three reagents attack. 3. Dinitrophenylation of these reactive SH groups is not the cause of inactivation, since active N-ethylmaleimide-substituted enzyme is also inactivated by Dnp-F.4. Complete inactivation of the N-ethylmaleimide-treated AMP deaminase occurs when about six tyrosine and two lysine residues are dinitrophenylated. 5. Since the treatment of Dnp-enzyme with 2-mercaptoethanol restores much of the enzyme activity, inactivation of AMP deaminase by Dnp-F is probably largely due to modification of tyrosine residues. 6. The kinetic properties of the Dnp-enzyme indicate that a marked decrease in V occurs only after extensive enzyme modification. The decreased activity after slight inactivation results from modification of Km.
Research Article|February 01 1975
The nature of inactivation of rat muscle 5'-adenylate aminohydrolase by fluorodinitrobenzene
Biochem J (1975) 145 (2): 145-151.
- Views Icon Views
- PDF LinkPDF
- Share Icon Share
- Cite Icon Cite
A Raggi, C Bergamini, G Ronca; The nature of inactivation of rat muscle 5'-adenylate aminohydrolase by fluorodinitrobenzene. Biochem J 1 February 1975; 145 (2): 145–151. doi: https://doi.org/10.1042/bj1450145
Download citation file: