Characterization of Membrane Proteins ofXanthomonas campestrispv.campestris

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Abstract
Total envelope proteins of X. campestris pv. [pathovar] campestris (hereafter referred to in this abstract as X. campestris) were purified by differential centrifugation of cells that were disrupted in a French pressure cell. The proteins were separated by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. Proteins of total envelopes of X. campestris presented a unique pattern when compared with profiles of proteins of other gram-negative rod-shaped bacteria, including other pathovars of X. campestris. There were 4 major bands of 62, 44, 26 and 23 K daltons and .apprx. 24 minor bands. Whereas no differences occurred in profiles of membranes of cells of different-aged cultures, differences were observed with a temperature shift from 30.degree. to 37.degree. C. Two proteins, the 44-kdalton major polypeptide and a 107-kdalton polypeptide, were heat modifiable.