A serum protein SP40,40 modulates the formation of membrane attack complex of complement on erythrocytes.

@article{Choi1989ASP,
  title={A serum protein SP40,40 modulates the formation of membrane attack complex of complement on erythrocytes.},
  author={Nak Hee Choi and Toshio Mazda and Motowo Tomita},
  journal={Molecular immunology},
  year={1989},
  volume={26 9},
  pages={835-40}
}
SP40,40 was isolated from the soluble membrane attack complex (SC5b-9) by HPLC using a reverse-phase column. Amino acid compositions of its alpha- and beta-subunits were similar to each other with the exception of glycine content. Amino-terminal sequences of its alpha- and beta-subunits were identical to those of the subunits prepared from human serum, respectively, indicating that there was no degradation of SP40,40 during incorporation into SC5b-9. When guinea pig erythrocytes were incubated… CONTINUE READING