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Physiology and Molecular Biology of Plants

, Volume 25, Issue 1, pp 243–251 | Cite as

Purification of a ribosome-inactivating protein with antioxidation and root developer potencies from Celosia plumosa

  • Ashraf GholizadehEmail author
Research Article
  • 29 Downloads

Abstract

Considering Celosia plumosa as a potent antiviral plant, the attempt was made to determine, purify and characterize its proteinaceous antiviral elements against tobacco mosaic virus hypersensitive response on Nicotiana glutinosa. By using 60% ammonium sulphate-precipitation, FPLC-based anion and cation-exchange chromatography in 10 and 50 mM NaCl, size-exclusion chromatography in 50 mM NaCl and SDS–PAGE 10%, a 25 kD antiviral protein with ribosome-inactivating/28S rRNase ability was purified from the leaves of C. plumosa at vegetative growth stage. The purified protein showed FRAP-based antioxidant activity in vitro and caused 1.7-fold and 1.4-fold increases in the growth rate of root system upon carborundum-based application on the root growth medium of N. glutinosa. The present work reports an antiviral protein with ribosome-inactivating, antioxidation and root developer potencies in C. plumosa as an edible or ornamental plant that may be useful in health and agricultural biotechnology in the future.

Keywords

Antioxidant Antiviral Celosia plumosa Ribosome inactivating Root growth 

Abbreviations

FRAP

Ferric reducing antioxidant power

AVP

Antiviral proteins

RIP

Ribosome-inactivating proteins

TMV

Tobacco mosaic virus

BME

Beta mercaptoethanol

PVP

Polyvinylpyrrolidone

FPLC

Fast performance liquid chromatography

SDS

Sodium dodecyl sulphate

EGTA

Ethylene glycol tetraacetic acid

DTT

Dithiothreitol

BSA

Bovine serum albumin

Notes

Acknowledgements

The author of this paper is thankful to Iran National Science Foundation (INSF), Tehran and Research Institute for Fundamental Sciences (RIFS), University of Tabriz, Iran for their funding and providing facilities for the present research work.

Funding

Iran National Science Foundation, Tehran, Iran (Grant No. 88001730).

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Copyright information

© Prof. H.S. Srivastava Foundation for Science and Society 2018

Authors and Affiliations

  1. 1.Iran National Science Foundation (INSF)TehranIran
  2. 2.Department of Biology, Research Institute for Fundamental Sciences (RIFS)University of TabrizTabrizIran

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