Purification and molecular properties of the toxin coded by Ustilago maydis virus P4.
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.
Department of Life Sciences, Indiana State University, Terre Haute 47809.
C
C
Ganesa
Y J
YJ
Chang
W H
WH
Flurkey
Z I
ZI
Randhawa
R F
RF
Bozarth
D000596:Amino Acids / Q000032:analysis; D001487:Basidiomycota; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D007526:Isoelectric Point; D008623:Mercaptoethanol / Q000494:pharmacology; D008970:Molecular Weight; D009183:Mycotoxins / Q000302:isolation & purification*; D012328:RNA Viruses / Q000378:metabolism*; D014588:Ustilago
D000596:Amino Acids; D009183:Mycotoxins; D008623:Mercaptoethanol