Abstract
We purified an iron-containing protein fromCampylobacter jejuni using ultracentrifugation and ionexchange chromatography. Electron microscopy of this protein revealed circular particles with a diameter of 11.5 nm and a central core with a diameter of 5.5 nm. The protein was composed of a single peptide of 21 kDa and did not serologically cross-react with horse spleen ferritin. The UV-visible spectrum of the protein showed no absorption peaks in the visible region, indicating that little or no heme is bound. The ratio of Fe:phosphate ofC. jejuni ferritin was 1.5∶1. From these morphological and chemical examinations, we concluded that theC. jejuni purified protein is a ferritin of the same class as that ofHelicobacter pylori andBacteroides fragilis and differs from the heme-containing bacterioferritin ofEscherichia coli. The 30 N-terminal amino acids were sequenced and were found to resemble the sequences of other ferritins strongly (H. pylori ferritin, 73% identity;B. fragilis ferritin, 50% identity;E. coli gene-165 product, 50% identity), and to a lesser degree, bacterioferritins (E. coli bacterioferritin, 26% identity;Azotobacter vinelandii, 26% identity; horse spleen ferritin 30% identity). Proteins that cross-reacted with antiserum against the ferritin ofC. jejuni were found in otherCampylobacter species and inH. pylori, but not inVibrio, E. coli, orPseudomonas aeruginosa.
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Wai, S.N., Takata, T., Takade, A. et al. Purification and characterization of ferritin fromCampylobacter jejuni . Arch. Microbiol. 164, 1–6 (1995). https://doi.org/10.1007/BF02568727
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DOI: https://doi.org/10.1007/BF02568727