Thermal Inactivation Properties of Enzymes from Typha latifolia L. Ecotypes | Zendy

S. J. McNaughton | Zendy

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Thermal Inactivation Properties of Enzymes from Typha latifolia L. Ecotypes

Author(s) -

S. J. McNaughton

Publication year - 1966

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.41.10.1736

Subject(s) - typha , citrate synthase , malate dehydrogenase , ecotype , enzyme , biology , aldolase a , botany , biochemistry , chemistry , ecology , wetland

Irreversible thermal denaturation experiments with 3 enzymes from Typha latifolia populations native to distinct thermal climates produced 3 different responses: (1) malate dehydrogenase was much more resistant to high temperature inactivation when obtained from plants native to a hot climate, (2) glutamate-oxaloacetate transaminase was quite resistant to thermal denaturation regardless of origin, and (3) aldolase was rapidly inactivated by heat regardless of origin.

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