Purification and characterization of an aspartyl proteinase from dry jack pine seeds
- 1 June 1991
- journal article
- research article
- Published by Cambridge University Press (CUP) in Seed Science Research
- Vol. 1 (3) , 139-147
- https://doi.org/10.1017/s0960258500000817
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
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