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Proteinases from buckwheat (Fagopyrum esculentum moench) seeds: Purification and properties of the 47 kDa enzyme

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Author(s): Timotijević Gordana S. | Radović Svetlana R. | Maksimović Vesna R.

Journal: Archives of Biological Sciences
ISSN 0354-4664

Volume: 58;
Issue: 3;
Start page: 171;
Date: 2006;
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Keywords: buckwheat | aspartic proteinase | pepstatin A affinity chromatography

ABSTRACT
Aspartic proteinases from buckwheat seeds are analyzed. Three forms of 47 kDa, 40 kDa and 28 kDa, were purified from mature buckwheat seeds, while two forms of 47 kDa and 28 kDa were detected in developing buckwheat seeds using pepstatin A affinity chromatography. A form of 47 kDa was selectively precipitated from other forms by ammonium sulfate precipitation. This enzyme resembles the chymosin-like pattern of proteolytic activity, as it was shown using BSA and k-casein as substrates, clarifying its ability for milk-clotting. The 47 kDa aspartic proteinase form is localized in the membrane fraction. .
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