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Plant Physiology 72:345-350 (1983)
© 1983 American Society of Plant Biologists

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Characterization of Soybean Endopeptidase Activity Using Exogenous and Endogenous Substrates 1

Heather M. Bond and Dianna J. Bowles

Department of Biochemistry, University of Leeds, Leeds, LS2 9JT United Kingdom

Endopeptidase activity in mature soybean seeds (Glycine max), has been measured using an exogenous substrate, [125I]iodoinsulin B chain. On the basis of pH optimum and the use of specific proteinase inhibitors, two distinct endopeptidase activities can be identified in both the embryonic axis and the cotyledons. One activity is characteristic of a neutral/alkaline metalloendopeptidase(s) and the other of an acidic carboxylendopeptidase(s). Neither activity is membrane-bound. The metalloendopeptidase(s), most probably working with neutral expopeptidases also present in the tissues, is capable of degrading certain subunits of the storage proteins. The beta subunit of conglycinin and additional seed polypeptides remain resistant to degradation. The carboxylpeptidase activity displayed a different specificity towards endogenous substrates; in particular, an acid-soluble polypeptide of apparent molecular weight 30,000 appeared to be the principal substrate for limited proteolytic degradation by the proteinase(s). Soybean agglutinin remained resistant to degradation by either class of endopeptidases.


1 This work was financially supported by an Science Research Council Grant A 97783 and B 73088 to Dr Dianna J. Bowles.




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K. Muntz, M.A. Belozersky, Y.E. Dunaevsky, A. Schlereth, and J. Tiedemann
Stored proteinases and the initiation of storage protein mobilization in seeds during germination and seedling growth
J. Exp. Bot., September 1, 2001; 52(362): 1741 - 1752.
[Abstract] [Full Text] [PDF]




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ASPB Publications PLANT PHYSIOLOGY THE PLANT CELL
Copyright © 1983 by the American Society of Plant Biologists