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Trypsin inhibitors in Pisum: variation in amount and pattern of accumulation in developing seed

Published online by Cambridge University Press:  19 September 2008

C. Domoney  and
T. Welham
C. Domoney*
Affiliation:
John Innes Institute, John Innes Centre for Plant Science Research, Colney Lane, Norwich NR4 7UH, UK
T. Welham
Affiliation:
John Innes Institute, John Innes Centre for Plant Science Research, Colney Lane, Norwich NR4 7UH, UK
*
* Correspondence
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Abstract

A survey of Pisum genotypes for seed trypsin inhibitors revealed a tenfold range in the extent of inhibition. Approximately 90% of trypsin inhibitory activity was associated with two albumin fractions in selected variant lines. The differences among extreme variants were consistent in three environments, between two sources of trypsin tested and whether expressed on a unit protein or dry weight basis.

A study of the appearance of trypsin inhibitors during seed development in selected highand low-inhibitor lines showed differences in the accumulation pattern of active inhibitors. An endogenous protease was identified in Pisum seed protein preparations, whose in vitro trypsin-like activity was predominant in protein from early stages of seed development, when little or no trypsin inhibitor was present. However, there was no correlation between the amount of this protease and the extent of trypsin inhibitory activity in lines that varied for inhibitor content.

Keywords

Pisumtrypsin inhibitorseed development
Type
Research Papers
Information
Seed Science Research , Volume 2 , Issue 3 , September 1992 , pp. 147 - 154
Copyright
Copyright © Cambridge University Press 1992

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