Identification of disulfide bonds in the ninth component (C9) of human complement

FEBS Letters
S LengweilerE E Rickli

Abstract

C9 is the most abundant protein of the membrane attack complex of complement. By means of limited proteolysis, different chromatographic techniques, a thiol-specific fluorescence assay, amino acid analysis, and Edman degradation 9 out of 12 disulfide bridges are definitely assigned (Cys22-Cys57, Cys33-Cys36, Cys67-Cys73, Cys121-Cys160, Cys233- Cys234, Cys359-Cys384, Cys489-Cys505, Cys492-Cys507, Cys509-Cys518). Weaker evidence permits to reduce the number of possible configurations for the remaining 3 cystines (Cys80-Cys91, Cys86-Cys104, Cys98-Cys113, or Cys80-Cys91, Cys86-Cys113, Cys98-Cys104). These findings are discussed in comparison with the strongly related components C6, C7, C8alpha, and C8beta.

References

Mar 19, 1991·Biochemistry·D HessE E Rickli
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Citations

Apr 2, 2011·The Journal of Biological Chemistry·Leslie L LovelaceLukasz Lebioda
Jul 28, 1999·Protein Science : a Publication of the Protein Society·J Y ChangP H Lai
Oct 16, 2008·Archives of Biochemistry and Biophysics·Jui-Yoa ChangRick A Wetsel

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