[Modification of the histidine in rat skeletal muscle deaminase by diethylpyrocarbonate].

Autor: Mardanian SS, Aĭrapetian RL, Arutiunian AV
Jazyk: ruština
Zdroj: Biokhimiia (Moscow, Russia) [Biokhimiia] 1996 Oct; Vol. 61 (10), pp. 1751-7.
Abstrakt: 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.
Databáze: MEDLINE