Studies Toward a Reversible Denaturation of Ribulose-1,5-Bisphosphate Carboxylase-Oxygenase from Puma Rye
Bouwens, Eric C.
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The reversible denaturation of ribulose-l,5-bisphosphate carboxylase-oxygenase from cold-hardened rye(Secale cereale L. cv Puma) was attempted by heating in solution at pH 8.6. Carboxylase activity was measured as a function of reaction temperature, 20 minute preincubation temperature, and incubation time at 46°C. Plots of the rate of apparent irreversible denaturation indicated second-order kinetics and initial aggregation of the enzyme to form dimers without significant formation of a partially uncoiled intermediate. The results are compared with the pseudo second-order kinetics observed during the thermal denaturation of bovine serum albumin for which a mechanism of denaturation is well established.