The Purification of a GroEL-Like Stress Protein from Aerobically Adapted Campylobacter jejuni

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Abstract

From plate cultures of Campylobacter jejuni grown in room air a particulate protein of 62 kDa was isolated by ion-exchange chromatography. The protein had a square shape from the side view but when viewed from the top it had a star-shaped structure. The molecular size of the whole particle determined by gel filtration was 850 kDa which suggested the presence of 14 subunits of 62 kDa in each particle. The N-terminal 37 amino residues showed more than 80% homology with the sequence of these heat shock protein (HSP) 60 homologs of Chlamydia trachomatis, Helicobacter pylori, and Escherichia coli (GroEL). This protein is immunologically cross-reactive with the antiserum for the 60-kDa HSP of Yersinia enterocolitica. Production of the 62-kDa protein increased under heat stress and growth in an aerobic atmospheric environment. From these observations we concluded that the 62-kDa protein is a Campylobacter stress protein (Cj62) which belongs to the HSP 60 family. © 1995, Center For Academic Publications Japan. All rights reserved.

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Takata, T., Ono, J., Amako, K., Nvunt Wai, S., Takade, A., & Sawae, Y. (1995). The Purification of a GroEL-Like Stress Protein from Aerobically Adapted Campylobacter jejuni. Microbiology and Immunology, 39(9), 639–645. https://doi.org/10.1111/j.1348-0421.1995.tb03245.x

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