Evidence for specific and non-covalent binding of lipids to natural and recombinant Mycobacterium bovis BCG hsp60 proteins, and to the Escherichia coli homologue GroEL.

@article{Bruyn2000EvidenceFS,
  title={Evidence for specific and non-covalent binding of lipids to natural and recombinant Mycobacterium bovis BCG hsp60 proteins, and to the Escherichia coli homologue GroEL.},
  author={Jean-Marc De Bruyn and Karine Soetaert and Pierre Buyssens and I Calonne and J L De Coene and Xavier Gallet and R. Brasseur and Ruddy Wattiez and Paul Falmagne and Henri Montrozier and Marie Antoinette Lan{\'e}elle and Mamadou Daff{\'e}},
  journal={Microbiology},
  year={2000},
  volume={146 ( Pt 7)},
  pages={1513-24}
}
Heat-shock proteins (Hsps) from various origins are known to share a conserved structure and are assumed to be key partners in the biogenesis of proteins. Fractionation of the mycobacterial Hsp60, a 65 kDa protein also called Cpn60, from Mycobacterium bovis BCG zinc-deficient culture filtrate on phenyl-Sepharose followed by Western blotting revealed the existence of four Hsp60-1 and Hsp60-2 forms, based on their hydrophobicity behaviour. Hsp60-2 species were further purified by ion-exchange… CONTINUE READING

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