Novel purification scheme and functions for a C3-binding protein from Streptococcus pneumoniae.

@article{Cheng2000NovelPS,
  title={Novel purification scheme and functions for a C3-binding protein from Streptococcus pneumoniae.},
  author={Qi Cheng and David Finkel and Margaret Kendrick Hostetter},
  journal={Biochemistry},
  year={2000},
  volume={39 18},
  pages={5450-7}
}
To isolate microbial proteins capable of binding the third component of complement (C3), we coupled the free sulfhydryl group of methylamine-inactivated C3 to a thiolSepharose matrix. This simple technique facilitated the purification of the first C3-binding protein isolated from a bacterium (Streptococcus pneumoniae). Both metastable (native) and thioester-disrupted C3 were recognized by this protein; binding of C3 was noncovalent, independent of thioester conformation, and preferential for… CONTINUE READING
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