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| Content Provider | Springer Nature Link |
|---|---|
| Author | Aliouane, Soumeya Pagès, Jean Marie Bolla, Jean Michel |
| Copyright Year | 2016 |
| Abstract | The Cj1169c-encoded putative protein of Campylobacter was expressed and purified from E. coli after sequence optimization. The purified protein allowed the production of a specific rabbit antiserum that was used to study the protein expression in vitro and its subcellular localization in the bacterial cell and putative interactions with other proteins. This protein is produced in Campylobacter and it clearly localizes into the periplasmic space. The level of protein production depends on factors, including pH, temperature, osmolarity, and growth phase suggesting a role in the Campylobacter environmental adaptation. The cysteine residues present in the sequence are probably involved in disulfide bridges, which may promote covalent interactions with other proteins of the Campylobacter envelope. |
| Starting Page | 511 |
| Ending Page | 517 |
| Page Count | 7 |
| File Format | |
| ISSN | 03438651 |
| Journal | Current Microbiology |
| Volume Number | 72 |
| Issue Number | 5 |
| e-ISSN | 14320991 |
| Language | English |
| Publisher | Springer US |
| Publisher Date | 2016-01-11 |
| Publisher Place | New York |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Microbiology Biotechnology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Medicine Microbiology Applied Microbiology and Biotechnology |
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