Purification and Characterization of a Family of High Molecular Weight Surface-Array Proteins from Campylobacter Fetus. (Reannouncement with New Availability Information).

摘要

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 weight(100,000, 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.