Purification and Characterization of a Family of High Molecular Weight Surface-Array Proteins from Campylobacter Fetus
VETERANS ADMINISTRATION MEDICAL CENTER DENVER CO
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A variety of Gram-negative and Gram-positive bacteria possess crystalline surface layers, although little is known of their function. We previously have shown that the high molecular weight surface-array proteins of Campylobacter fetus are important in both the pathogenicity and antigenicity of this organism. For biochemical and immunological characterization, we purified high molecular weight100,000, 127,000, 149,000 surface-array proteins from three C. fetus strains using sequential gel filtration and ion exchange high performanc liquid chromatography. These proteins are acidic with pl values between 4.12 and 4.25 and contain large proportions of acidic amino acids 19. 7-22.0 in addition to hydrophobic amino acids 37.3-38.5. They share a novel amino-terminal sequence through at least 19 residues.