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Purification and characterization of an aspartyl proteinase from dry jack pine seeds

Published online by Cambridge University Press:  19 September 2008

Jacqueline Bourgeois  and
L. Malek
Jacqueline Bourgeois
Affiliation:
Department of Biology, Lakehead University, Thunder Bay, Ontario, Canada P7B 5E1
L. Malek*
Affiliation:
Department of Biology, Lakehead University, Thunder Bay, Ontario, Canada P7B 5E1
*
* Correspondence
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Abstract

A high-molecular-weight aspartyl proteinase complex, sensitive to pepstatin A was purified to near electrophoretic homogeneity from dry seeds ofjack pine (Pinus banksiana, Lamb.). Two partial activities, endo-and exo-proteinolytic, were associated with the complex, judged by the analysis of haemoglobin hydrolysis products. The high activity of this enzyme in dry jack pine seed suggests a possible function in early germination.

Keywords

aspartyl (acid) proteinasedry seedenzyme purificationjack pine(Pinus banksiana)
Type
Research Papers
Information
Seed Science Research , Volume 1 , Issue 3 , September 1991 , pp. 139 - 147
Copyright
Copyright © Cambridge University Press 1991

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