Abstract
The major outer membrane proteins from two subspecies of the phytopathogenic bacterium Erwinia carotovora were characterized. Protein patterns of E. carotovora ssp. carotovora isolates showed considerable heterogeneity in respect to both minor and major proteins, whereas isolates of E. carotovora ssp. atroseptica were almost identical. All isolates studied contained only two major proteins with Mr values from 36 500 to 39 500. One of these major proteins resembled the OmpA protein of Escherichia coli: it was heat-modifiable and partially trypsin-sensitive, producing an Mr 24 000 tryptic fragment. The other major protein species showed properties characteristic of porin proteins: it was resistant to trypsin and could be isolated as a protein-peptidoglycan complex.
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