Literature DB >> 16656465

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

S J McNaughton1.   

Abstract

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.

Entities:  

Year:  1966        PMID: 16656465      PMCID: PMC550600          DOI: 10.1104/pp.41.10.1736

Source DB:  PubMed          Journal:  Plant Physiol        ISSN: 0032-0889            Impact factor:   8.340


  1 in total

1.  THE TEMPERATURE DEPENDENCE OF MYOSIN-ADENOSINETRIPHOSPHATASE AND ALKALINE PHOSPHATASE IN LIZARDS.

Authors:  P LICHT
Journal:  Comp Biochem Physiol       Date:  1964-07
  1 in total
  3 in total

1.  The productive and reproductive biology of flowering plants : VII. resource allocation and reproductive capacity in wild populations of Heloniopsis orientalis (Thunb.) C. Tanaka (Liliaceae).

Authors:  Shoichi Kawano; Junzo Masuda
Journal:  Oecologia       Date:  1980-01       Impact factor: 3.225

2.  Adaptation of malate dehydrogenase to environmental temperature variability in two populations of Potentilla glandulosa Lindl.

Authors:  J A Terri; M M Peet
Journal:  Oecologia       Date:  1978-01       Impact factor: 3.225

3.  Preadaptation of protein synthesis in wheat seedlings to high temperature.

Authors:  M Weidner; C Ziemens
Journal:  Plant Physiol       Date:  1975-11       Impact factor: 8.340

  3 in total

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