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Protein disulfide isomerase in germinating wheat (Triticum aestivum) seed and during loss of viability

Published online by Cambridge University Press:  19 September 2008

M. A. Livesley ,
N. J. Bulleid  and
C. M. Bray
M. A. Livesley
Affiliation:
Department of Biochemistry and Molecular Biology, University of Manchester, Oxford Road, Manchester M13 9PT, UK
N. J. Bulleid
Affiliation:
Department of Biochemistry and Molecular Biology, University of Manchester, Oxford Road, Manchester M13 9PT, UK
C. M. Bray*
Affiliation:
Department of Biochemistry and Molecular Biology, University of Manchester, Oxford Road, Manchester M13 9PT, UK
*
* Correspondence
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Abstract

Protein disulfide isomerase (PDI E.C. 5.3.4.1) catalyses the formation of disulfide bonds in secretory or cell-surface proteins during their biosynthesis. PDI activity is associated with the microsomal fraction of the cell and has been found in several mammalian tissues and in developing wheat endosperm.

The embryo and aleurone layer of germinating seeds of the wheat cultivar Galahad showed PDI activity associated with a microsome-enriched fraction of cell homogenates PDI activity in microsome-enriched fractions from aleurone layers of normally germinating seeds was significantly higher than in their abnormally germinating counterparts and diminished as germination proceeded.

Dry embryos and germinating embryos showed less PDI activity than aleurone layers. There was no significant difference in PDI activity between microsome-enriched fractions from embryos of normally and abnormally germinating seeds at 3 or 6 days of germination.

Wheat aleurone PDI was partially purified using gel filtration and had a molecular mass of 110–130 kDa and a monomeric molecular mass of ca. 57 kDa on sodium dodecyl sulfate polyacrylamide gel electrophoresis.

Keywords

aleuroneembryoprotein foldingprotein disulfide isomerasewheat
Type
Research Papers
Information
Seed Science Research , Volume 2 , Issue 2 , June 1992 , pp. 97 - 103
Copyright
Copyright © Cambridge University Press 1992

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