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Purification and molecular properties of the toxin coded by Ustilago maydis virus P4.

Authors :
Ganesa C
Chang YJ
Flurkey WH
Randhawa ZI
Bozarth RF
Source :
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 1989 Jul 31; Vol. 162 (2), pp. 651-7.
Publication Year :
1989

Abstract

The toxin from the P4 strain of Ustilago maydis was purified and characterized using a series of gel-filtration and ion-exchange columns. The apparent molecular weight of the purified toxin was estimated from gel electrophoresis to be 11.3 kd in the presence of 2-mercaptoethanol and 10.3 kd in the absence of 2-mercaptoethanol. Amino acid analysis indicated 12% basic amino acids, 14% acidic amino acids and 16% glycine. The toxin was also stable to filtration and repeated freezing at -20 degrees C and thawing.

Details

Language :
English
ISSN :
0006-291X
Volume :
162
Issue :
2
Database :
MEDLINE
Journal :
Biochemical and biophysical research communications
Publication Type :
Academic Journal
Accession number :
2757636
Full Text :
https://doi.org/10.1016/0006-291x(89)92360-7