The Purification and Properties of One of the ‘b’ Proteins from Virus-Infected Tobacco Plants

A - Papers appearing in refereed journals

Antoniw, J. F. and Pierpoint, W. S. 1978. The Purification and Properties of One of the ‘b’ Proteins from Virus-Infected Tobacco Plants. Journal of General Virology. 39 (2), pp. 343-350.

AuthorsAntoniw, J. F. and Pierpoint, W. S.
Abstract

The b1 protein, produced in leaves of Nicotiana tabacum cv. Xanthi-nc following infection with tobacco mosaic virus, has been purified to homogeneity by a procedure which involves gel chromatography and absorption on to DEAE-cellulose. One gel chromatography step was sufficient when the procedure was applied to leaf extracts made in an acid buffer, whereas two were necessary with extracts made at pH 8. The final product migrates as a single protein band on electrophoresis in both acrylamide and SDS-acrylamide gels. Its mol. wt. is estimated to be 15000 by electrophoresis and 14200 by ultracentrifugation. Amino acid analysis suggests that it contains about 136 residues of which 39 are potentially acidic, 13 basic and 16 aromatic. The absorbance coefficient A 1% 280 nm is estimated to be 18.9. No evidence was found for the presence of a nucleotide component.

Year of Publication1978
JournalJournal of General Virology
Journal citation39 (2), pp. 343-350
Digital Object Identifier (DOI)doi:10.1099/0022-1317-39-2-343
Open accessPublished as bronze (free) open access
Publisher's version
Output statusPublished
Publication dates
Print01 May 1978
Publication process dates
Accepted01 Dec 1977
Copyright licensePublisher copyright
ISSN0022-1317
PublisherMicrobiology Society

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