Antipeptide monoclonal antibodies to defined fibrinogen Aα chain regions : Anti-Aα 487-498, a structural probe for fibrinogenolysis

• Published in: Blood 1998-03, Vol.91 (5), p.1590-1598
• Main Authors: SOBEL, J. H, TRAKHT, L, PILEGGI, N, HONG QI WU
• Format: Article
• Language: English
• Subjects: Biological and medical sciences; Blood coagulation. Blood cells; Fundamental and applied biological sciences. Psychology; General aspects, investigation methods, hemostasis, fibrinolysis; Molecular and cellular biology
• ISSN: 0006-4971; 1528-0020
• DOI: 10.1182/blood.v91.5.1590

The fibrinogen αC domain (Aα 220-610) is one of the earliest targets attacked by plasmin following fibrinolytic system activation. Monoclonal antibodies (MoAbs) to defined sequences within the αC domain provide the opportunity to explore the structure-function relationships involved in plasmin's interaction with its Aα chain substrate at greater resolution and can serve as reagents with potential clinical use for detecting fibrinogenolysis in vivo. The MoAb F-104 was raised against a multiple antigenic peptide derivative modelled after the hydrophilic 12-residue sequence corresponding to Aα 487-498 within the αC domain. A sensitive solution phase competitive enzyme-linked immunosorbent assay (ELISA) was developed for MoAb F-104 that can be applied for the direct measurement of intact fibrinogen (purified or plasma; ED50%≈5 pmol Aα chain equivalents/mL), with negligible cross-reactive interference from peptide cleavage products released by plasmin from the COOH-terminal end of the Aα chain (