Radiation Inactivation of Rabbit Muscle Aldolase

Abstract
Pulse radiolysis and steady-state X-radiolysis have been used to investigate the radiation inactivation of aldolase from rabbit muscle. Both eaq and OH readily react with aldolase, and contribute to inactivation. The radical anions (CNS)2 and (Br)2 react with aldolase at neutral pH. The progressive addition of alkali results in an increase in the second-order rate constants, with an apparent pK ∼ 10 ± 0·3, and with the formation of an unstable intermediate, λmax ∼400 nm resembling a phenoxyl radical. Steady-state radiolysis in the presence of (CNS)2 and (Br)2 at alkaline pH results in increased aldolase inactivation, with a pK of enzyme inactivation similar to that observed for reaction of the radical anions. We propose that a reaction of the radical anions with tyrosine residues accounts for the resultant inactivation.