Hui K Y, Haber E, Matsueda G R
Hybridoma. 1986 Fall;5(3):215-22. doi: 10.1089/hyb.1986.5.215.
Three monoclonal antibodies (MAbs) (55D10, 59D8, and 64C5) have been produced by an immunization strategy that uses a synthetic heptapeptide from the amino terminus of the beta-chain in human fibrin. These MAbs bind to human fibrin in the presence of 4 mg/ml human fibrinogen in solid-phase radioimmunoassay. Ligand specificity studies demonstrate that antifibrin immunoreactivity is completely inhibited by a series of synthetic fibrin-like beta-peptides that bear the position-2 histidyl residue. Although the presence of this residue on the epitope is necessary for its recognition by a fibrin-specific antibody, the presence of the histidyl residue alone is not sufficient for antibody recognition.
通过一种免疫策略制备了三种单克隆抗体(MAb)(55D10、59D8和64C5),该策略使用了来自人纤维蛋白β链氨基末端的合成七肽。在固相放射免疫分析中,这些单克隆抗体在存在4mg/ml人纤维蛋白原的情况下与人纤维蛋白结合。配体特异性研究表明,抗纤维蛋白免疫反应性被一系列带有2位组氨酸残基的合成纤维蛋白样β肽完全抑制。尽管该表位上此残基的存在对于其被纤维蛋白特异性抗体识别是必要的,但仅组氨酸残基的存在不足以实现抗体识别。