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