Purification of the fourth, second and fifth components of mouse complement.

@article{Fukuoka1984PurificationOT,
  title={Purification of the fourth, second and fifth components of mouse complement.},
  author={Yoshiko Fukuoka and J Seino and Tomohiko Okuda and Takehiko Tachibana},
  journal={Immunology},
  year={1984},
  volume={51 3},
  pages={493-501}
}
The fourth, second and fifth components of mouse complement were purified by a combination of polyethylene glycol precipitation, ion exchange chromatography and gel filtration. The final products were homogeneous on SDS-PAGE, and the activity yields were 8.5% for C4, 32% for C2 and 40% for C5. C4 was composed of three polypeptide chains with mol. wts of 90,000, 78,000 and 32,000. C2 was composed of a single polypeptide chain with a mol. wt. of 115,000 and cleaved by C1s into two fragments with… CONTINUE READING