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The region Ser333-Arg356 of the alpha-chain of human C4b-binding protein is involved in the binding of complement C4b

  • M. Hessing
  • , D. Kanters
  • , H. Takeya
  • , C. van 't Veer
  • , T. M. Hackeng
  • , S. Iwanaga
  • , B. N. Bouma

Research output: Contribution to journalArticleAcademicpeer-review

Abstract

Human C4b-binding protein (C4BP) functions as a cofactor to factor I in the degradation of C4b and accelerates the decay rate of the C4b2a complex. In this study we describe a monoclonal antibody directed against the alpha-chain of C4BP that inhibits the binding of C4b to C4BP. In order to identify the structural domain of the alpha-chain of C4BP that interacts with C4b, tryptic fragments of C4BP were generated. Amino acid sequence analysis of the fragments revealed that the residues Ser333-Arg356 of the alpha-chain of C4BP contain the epitope of this antibody, and as a consequence, that this part of the alpha-chain of C4BP is likely to be involved in the interaction with C4b
Original languageEnglish
Pages (from-to)228-232
JournalFEBS letters
Volume317
Issue number3
DOIs
Publication statusPublished - 1993

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