[Modification of the histidine in rat skeletal muscle deaminase by diethylpyrocarbonate].
Diethylpyrocarbonate inactivated rat skeletal muscle AMP deaminase in 10 mM phosphate buffer, pH 6.5, at 23 degrees with the second order rate constant of 580 M-1.min-1. Absorbtion at 240 nm was concomitantly increase. Enzyme activity can be restored by hydroxylamine. The pH-dependence of inactivation indicates the involvement of a group with pKa 6.9. The data suggest that modification of one histidyl residue per subunit inactivates the activity of tetrameric AMP deaminase.
Mardanian
S S
SS
Aĭrapetian
R L
RL
Arutiunian
A V
AV
D000659:AMP Deaminase / Q000737:chemistry* / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D004047:Diethyl Pyrocarbonate / Q000737:chemistry*; D006639:Histidine / Q000737:chemistry*; D018482:Muscle, Skeletal / Q000201:enzymology*; D051381:Rats
D006639:Histidine; D000659:AMP Deaminase; D004047:Diethyl Pyrocarbonate