Apyrase, streptavidin-binding proteins, and antimicrobial activity in Pisum sativum

Apyrase, streptavidin-binding proteins, and antimicrobial activity in Pisum sativum The 49 kD apyrase (EC 3.6.1.5), streptavidin-binding proteins, and antimicrobial activity in the subcellular fractions from different seed parts of Pisum sativum L. var. Alaska were examined. Except cotyledons, all subcellular fractions contained 49 kD apyrase, and a considerable relationship was found between 49 kD apyrase and NTPase activities that increased with increasing time of germination. The bulk of 49 kD apyrase and NTPase activities was found in the nucleus pellets and cytoskeleton-enriched fraction, indicating their physiological importance. At 72 h of germination, all subcellular fractions of primary stems have a greater amount of 49 kD apyrase and NTPase than primary leaves and much more than primary roots and cotyledonary stalks. All seed parts showed antimicrobial activities, and the bulk of inhibition activities was found in the cytoskeleton-enriched and nucleus pellets, which was greater in the primary stems and leaves than in other parts. Current findings reveal that apyrases have important roles in metabolic activities in all parts of the pea plants except cotyledons. Cotyledons contained much streptavidin-binding proteins, which might have different physiological roles than apyrases. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Russian Journal of Plant Physiology Springer Journals

Apyrase, streptavidin-binding proteins, and antimicrobial activity in Pisum sativum

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Publisher
Pleiades Publishing
Copyright
Copyright © 2014 by Pleiades Publishing, Ltd.
Subject
Life Sciences; Plant Physiology; Plant Sciences
ISSN
1021-4437
eISSN
1608-3407
D.O.I.
10.1134/S102144371404013X
Publisher site
See Article on Publisher Site

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