Soluble mycelial proteins from Ophiostoma ulmi (Buism.) Nannf., the causal agent of Dutch elm disease, were separated by analytical electrofocusing and two-dimensional electrophoresis in polyacrylamide gels. Results showed the aggressive and nonaggressive strains of this pathogen each had about 60 Coomassie blue stained bands having isoelectric points from 3 to 7. Both strains of this fungus had their own characteristic electrofocusing patterns. Nonaggressive isolate S116, for example, lacked two protein bands, one near the anode and one near the cathode, but it had five additional protein bands distributed from pH 4 to 6. Two-dimensional electrophoresis of total soluble proteins depicted that there were 36 proteins found to be specific for the nonaggressive isolate S116 and 12 proteins for the aggressive isolate RR2.
High resolution two-dimensional electrophoresis of proteins.
