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

Autor:	Jacqueline Bourgeois, L. Malek
Rok vydání:	1991
Předmět:	chemistry.chemical_classification fungi food and beverages Plant Science Pinus Haemoglobin hydrolysis Jack pine chemistry.chemical_compound Horticulture Enzyme Biochemistry chemistry Germination High activity Pepstatin
Zdroj:	Seed Science Research. 1:139-147
ISSN:	1475-2735 0960-2585
DOI:	10.1017/s0960258500000817
Popis:	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.
Databáze:	OpenAIRE
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