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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

Author: Hessing, M. · Kanters, D. · Takeya, H. · Veer, C. van 't · Hackeng, T.M. · Iwanaga, S. · Bouma, B.N.
Type:article
Date:1993
Institution: Centraal Instituut voor Voedingsonderzoek TNO
Source:FEBS Letters, 3, 317, 228-232
Identifier: 80343
doi: doi:10.1016/0014-5793(93)81281-4
Keywords: Amino Acid Sequence · Antibodies, Monoclonal · Carrier Proteins · Complement 4b · Electrophoresis, Polyacrylamide Gel · Human · Immunoblotting · Molecular Sequence Data · Peptide Mapping · Receptors, Complement

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 α-chain of C4BP that inhibits the binding of C4b to C4BP. In order to identify the structural domain of the α-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 α-chain of C4BP contain the epitope of this antibody, and as a consequence, that this part of the α-chain of C4BP is likely to be involved in the interaction with C4b. Chemicals/CAS: complement component C4b, 80295-50-7; Antibodies, Monoclonal; Carrier Proteins; Complement 4b, 80295-50-7; complement 4b-binding protein; Receptors, Complement