Thermal Inactivation Properties of Enzymes from Typha latifolia L. Ecotypes
- 1 December 1966
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 41 (10) , 1736-1738
- https://doi.org/10.1104/pp.41.10.1736
Abstract
Irreversible thermal denaturation experiments with 3 enzymes from Typha latifolia populations native to distinct thermal climates produced 3 different responses: malate dehydrogenase (EC 1.1.1.37) was much more resistant to high temperature inactivation when obtained from plants native to a hot climate: glutamate-oxaloacetate transaminase (EC 2.6.1.1) was quite resistant to thermal denaturation regardless of origin; and aldolase (EC 4.1.2.b) was rapidly inactivated by heat regardless of origin.This publication has 1 reference indexed in Scilit:
- The temperature dependence of myosin-adenosinetriphosphatase and alkaline phosphatase in lizardsComparative Biochemistry and Physiology, 1964