J. Biol. Chem., Vol. 255, Issue 22, 10764-10770, 11, 1980
A kinetic study on the diffusion-coupled reaction of a basic horseradish peroxidase adsorbed on the carboxymethylcellulose membrane
T Ishikawa, M Tamura and I Yamazaki
The rate of reactions of a basic horseradish peroxidase adsorbed on the
carboxymethylcellulose membrane was measured spectrophotometrically by
monitoring the state of the enzyme. For the reactions with hydrogen
peroxide and cyanide dissolved in media the diffusion process was rate
limiting both in the static and flowing media, and kinetic features of the
enzyme were masked. The rate of CO recombination of the ferrous enzyme was
measured by flash photolysis in the static media containing varying amounts
of CO. Apparently, the initial rate of CO recombination was no more
affected by the diffusion factor, and the second order rate constant could
be measured for the reaction of the enzyme adsorbed on the membrane. The
value was about 70% of that obtained from the enzyme in solution and
exhibited the same pH dependence as did the value for the enzyme in
solution. The difference of the reaction pattern between the enzymes on the
membrane and in solution became distinct when flash photolysis was applied
to the reaction system without free CO in the medium. The kinetic data were
analyzed by computer simulation.
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