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The sequence γ-(312-324) is a fibrin-specific epitope

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Author: Schielen, W.J.G. · Adams, H.P.H.M. · Leuven, K. van · Voskuilen, M. · Tesser, G.I. · Nieuwenhuizen, W.
Type:article
Date:1991
Institution: Gaubius Instituut TNO
Source:Blood, 10, 77, 2169-2173
Identifier: 231435
Keywords: Amino Acid Sequence · Amino Acids · Antibodies, Monoclonal · Antibody Specificity · Enzyme-Linked Immunosorbent Assay · Epitopes · Fibrin · Human · Molecular Sequence Data · Peptide Fragments

Abstract

Fibrin accelerates the activation of plasminogen catalyzed by tissue-type plasminogen activator much stronger than fibrinogen. Detailed studies showed that (part of) this rate-enhancing effect of fibrin is brought about by two sites in the fibrin molecule: one in Aα-(148-160) and one in the γ-chain stretch 311-379 (also known as FCB-5). During the fibrinogen-to-fibrin conversion, Aα-(148-160) appears to become accessible, because a monoclonal antibody against synthetic Aα-(148-160) reacts with fibrin, but not with fibrinogen. Because a similar situation may exist for (at least parts of) FCB-5, we have prepared a monoclonal antibody against a part (ie, γ-[312-324]) of FCB-5, and found that this is fibrin-specific and does not bind fibrinogen. We conclude that γ-(312-314) is hidden in fibrinogen and is exposed by the formation of fibrin. Chemicals/CAS: fibrin, 9001-31-4; fibrinogen, 9001-32-5; Amino Acids; Antibodies, Monoclonal; Epitopes; Fibrin, 9001-31-4; Peptide Fragments