Studies Toward a Reversible Denaturation of Ribulose-1,5-Bisphosphate Carboxylase-Oxygenase from Puma Rye
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Authors
Bouwens, Eric C.
Issue Date
1979
Type
Thesis
Language
en_US
Keywords
Alternative Title
Abstract
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.
Description
Citation
Publisher
Kalamazoo College
License
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