| synthesis and processing of killer toxin from ustilago maydis virus p4. | the synthesis of toxin protein from ustilago maydis virus (umv) strain p4 was studied in vitro and in vivo. the protein synthesized in vitro and in vivo has a molecular weight of approximately 30 kd whereas the native toxin has a molecular weight of about 12 kd. in the presence of protease inhibitors and glycosylation inhibitors, toxin protein synthesized in vivo showed higher molecular weight products that could be immunoprecipitated with toxin antibodies. these results suggest that the umv p4 ... | 1987 | 3426580 |
| 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 ... | 1989 | 2757636 |
| ustilago maydis virus p4 killer toxin: characterization, partial amino terminus sequence, and evidence for glycosylation. | the toxin from ustilago maydis virus p4 was purified to homogeneity and characterized. the native molecular mass, using size-exclusion hplc was estimated to be 7.2 kda. the purified toxin was composed of a single subunit. sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis under reduced and nonreduced conditions resulted in estimated molecular masses of 8.4 and 7.4 kda, respectively. the purified toxin was found to be glycosylated when tested for carbohydrates using the phenol-sul ... | 1991 | 1897946 |