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

Russian Journal of Plant Physiology volume 61, pages 496–502 (2014)Cite this article

Abstract

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.

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Abbreviations

BCIP:

5-bromo-4-chloro-3-indolyl phosphate

BPB:

bromophenol blue

CSB:

cytoskeleton-stabilizing buffer

DMSO:

dimethyl sulfoxide

NBT:

nitro blue tetrazolium

PMSF:

phenylmethylsulfonyl fluoride

PTE:

polyoxyethylene-10-tridecyl ether

SBP:

streptavidin-binding protein

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Authors and Affiliations

  1. Botany Department, Faculty of Science, South Valley University, ??, Egypt

    M. F. M. Moustafa

  2. Department of Biological Science, Faculty of Sciences, King Khalid University, Abha, Saudi Arabia

    M. F. M. Moustafa

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  1. M. F. M. Moustafa
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Correspondence to M. F. M. Moustafa.

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Moustafa, M.F.M. Apyrase, streptavidin-binding proteins, and antimicrobial activity in Pisum sativum . Russ J Plant Physiol 61, 496–502 (2014). https://doi.org/10.1134/S102144371404013X

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  • DOI: https://doi.org/10.1134/S102144371404013X

Keywords

  • Pisum sativum
  • 49 kD apyrase
  • streptavidin-binding proteins
  • antimicrobial activity