Structural characterization of the C4a anaphylatoxin from rat

Mol Immunol. 1988 Jul;25(7):663-71. doi: 10.1016/0161-5890(88)90101-0.


The C4a anaphylatoxin was purified from rat sera activated by heat-aggregated IgG. The anaphylatoxin was isolated by a three-step purification procedure and was judged to be homogeneous based on visualization of a single stained band after electrophoresis on both cellulose acetate membrane strips and on 9% SDS-polyacrylamide gels. Results from Ouchterlony and radioimmunoassay analysis indicated that neither rat C5A nor C3a contaminated the C4a preparation. Rat C4a is a glycoprotein estimated to be 11,000-12,000 mol. wt and contains 76 amino acid residues representing a mol. wt of 8577 and one oligosaccharide unit of 2000-3000 mol. wt. Rat C4a is weakly active in contracting guinea pig ileum at 0.1-1 microM, which is comparable with the activity of human C4a. Both human and bovine C4a are polypeptides free of carbohydrate while rat and presumably mouse C4a are glycoproteins. The complete primary structure of rat C4a anaphylatoxin has been elucidated as follows: (formula; see text)

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Anaphylatoxins* / isolation & purification
  • Animals
  • Complement C4* / isolation & purification
  • Complement C4a
  • Molecular Sequence Data
  • Peptides*
  • Rats


  • Anaphylatoxins
  • Complement C4
  • Peptides
  • Complement C4a