Structure of the IgG-binding regions of streptococcal protein G.

@article{Guss1986StructureOT,
  title={Structure of the IgG-binding regions of streptococcal protein G.},
  author={Bengt Guss and Mona Eliasson and Annika Ohrfelt Olsson and Mathias Uhl{\'e}n and A K Frej and Hans J{\"o}rnvall and J. I. Flock and Martin Lindberg},
  journal={The EMBO journal},
  year={1986},
  volume={5 7},
  pages={1567-75}
}
The gene encoding the IgG-binding protein G from Streptococcus G148 was isolated by molecular cloning. A subclone containing a 1.5-kb insert gave a functional product in Escherichia coli. Protein analysis of affinity-purified polypeptides revealed two gene products, both smaller than protein G spontaneously released from streptococci, but with identical IgG-binding properties. The complete nucleotide sequence of the insert revealed a repeated structure probably evolved through duplications of… CONTINUE READING
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