Purification and characterization of ferritin fromCampylobacter jejuni |
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Authors: | Sun Nyunt Wai Tohru Takata Akemi Takade Naotaka Hamasaki Kazunobu Amako |
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Institution: | (1) Department of Bacteriology, Faculty of Medicine, Kyushu University, 3-1–1 Maidashi, Higashi-ku, Fukuoka 812, Japan Tel. +81-092-641-1151 (Ext. 3406); Fax +81-092-632-6402 e-mail amako@bact.med.kyushu-u.ac.jp, JP;(2) Department of Clinical Chemistry and Laboratory Medicine, Kyushu University, Fukuoka 812, Japan, JP |
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Abstract: | We purified an iron-containing protein from Campylobacter jejuni using ultracentrifugation and ion-exchange 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 of C. jejuni ferritin was 1.5:1. From these morphological and chemical examinations, we concluded that the C. jejuni purified protein is a ferritin of the same class as that of Helicobacter pylori and Bacteroides fragilis and differs from the heme-containing bacterioferritin of Escherichia 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 of C. jejuni were found in other Campylobacter species and in H. pylori, but not in Vibrio, E. coli, or Pseudomonas aeruginosa.
Received: 6 September 1994 / Accepted: 6 February 1995 |
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Keywords: | Campylobacter jejuni Iron-containing protein Ferritin |
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