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Isolation and characterization of a heat-soluble protein from pea (Pisum sativum) embryos

Published online by Cambridge University Press:  19 September 2008

Pauline S. Russouw ,
Jill Farrant ,
Wolf Brandt ,
Dennis Maeder  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
Dennis Maeder
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

An LEA-like protein has been isolated and characterized from pea (Pisum sativum) embryos. It is the most prevalent protein in a homogenate of pea axes heated for 10 min at 80°C and then centifuged for 10 min at 17000 g (80°C supernatant fraction). It has a molecular mass of 11 kDa and is very rich in hydrophilic amino acids, notably aspartate, glutamate and glycine. The protein is not recognized by an antibody to the group II dehydrin C-terminal consensus sequence. Antibodies to the isolated protein recognize a number of larger proteins in the 80°C supernatant fraction of pea and other legumes (chick pea, soybean and bean) as well as gramineous seeds (wheat, maize and barley). The protein undergoes a substantial increase in α-helical content at high ionic strength but does not dimerize.

Keywords

DesiccationLEA proteinpea embryosprotein characterization

Information

Type
Physiology and Biochemistry
Information
Seed Science Research , Volume 5 , Issue 3 , September 1995 , pp. 137 - 144
Copyright
Copyright © Cambridge University Press 1995

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