Purification and partial characterization of antiviral proteins from Chenopodium album L. leaves

Citation
S. Dutt et al., Purification and partial characterization of antiviral proteins from Chenopodium album L. leaves, J PLANT PHY, 156(5-6), 2000, pp. 808-810
Citations number
17
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Plant Sciences","Animal & Plant Sciences
Journal title
JOURNAL OF PLANT PHYSIOLOGY
ISSN journal
0176-1617 → ACNP
Volume
156
Issue
5-6
Year of publication
2000
Pages
808 - 810
Database
ISI
SICI code
0176-1617(200005)156:5-6<808:PAPCOA>2.0.ZU;2-U
Abstract
Two antiviral proteins from leaves of Chenopodium album L, have been purifi ed and their characteristics compared. Both of these impart resistance in h ypersensitive hosts: against tobacco mosaic virus in Nicotiana tabacum cv. Samsun NN and N. glutinosa, and sunnhemp rosette virus in Cyamopsis tetrago noloba. One of them exhibited a single polypeptide with a molecular mass of 25 kD, and the other one is a complex showing polypeptide bands of 27, 25 and 18kD on SDS-PAGE. The 25 kD protein and the complex protein inhibited m ore than 90 % lesion formation at a concentration of 20-22 mu g mL(-1). Bot h of the proteins are basic in nature and can tolerate high temperature (up to 90 degrees C).