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The most prevalent protein in a heat-treated extract of pea (Pisum sativum) embryos is an LEA group I protein; its conformation is not affected by exposure to high temperature

Published online by Cambridge University Press:  19 September 2008

Pauline S. Russouw ,
Jill Farrant ,
Wolf Brandt  and
George G. Lindsey
Pauline S. Russouw
Affiliation:
Department of Biochemistry, University of Cape Town, Private Bag, Rondebosch 7700, South Africa
Jill Farrant
Affiliation:
Department of Botany, University of Cape Town, Private Bag, Rondebosch 7700, South Africa
Wolf Brandt
Affiliation:
Department of Biochemistry, University of Cape Town, Private Bag, Rondebosch 7700, South Africa
George G. Lindsey*
Affiliation:
Department of Biochemistry, University of Cape Town, Private Bag, Rondebosch 7700, South Africa
*
*Correspondence
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Abstract

The LEA-like protein previously isolated from a homogenate of pea (Pisum sativum L.) embryonic axes heated at 80°C for 10 min (Russouw et al., 1995) was purified without exposure to heat. Peptides produced by trypsin digestion were separated by HPLC and sequenced. The protein was identified as a member of the LEA group I family. The conformation of the protein was compared before and after heat treatment by antibody affinity, circular dichroism spectroscopy, fluorescence spectroscopy and 8-anilino-1-naphthalenesulfonic acid binding. No differences could be detected, demonstrating that the protein was not irreversibly denatured by exposure to high temperature.

Keywords

denaturationembryosheatLEA proteinpeas
Type
Biochemistry and Metabolism
Information
Seed Science Research , Volume 7 , Issue 2 , June 1997 , pp. 117 - 124
Copyright
Copyright © Cambridge University Press 1997

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