Abstract
Eighteen mouse hybridomas secreting monoclonal antibodies (mAbs) to human serum amyloid P-component (SAP) were prepared and characterized. The relative avidities of purified mAbs for Human SAP (HuSAP) ranged from 0.05 to 3.3 μg/ml. The mAbs were assigned to three groups on the basis of epitope specificity determined by competitive inhibition. In group I (13 mAbs) nine mAbs bind to native HuSAP only and four bind to native and denatured HuSAP. The four mAbs comprising group II recognize native and denatured HuSAP. One m Ab only comprises Group III. Seven mAbs were tested for their ability to precipitate iodinated HuSAP from solution. The m Ab from Group III does not precipitate. Eleven out of twelve mAbs, tested by gel immunodiffusion precipitate HuSAP in a calcium independent manner. Calcium is not required for recognition of HuSAP by any of the monoclonals.
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© 1991 Springer Science+Business Media Dordrecht
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O’Sullivan, G., Mcadam, K.P.W.J., Raynes, J.G. (1991). Monoclonal Antibodies to Human Serum Amyloid P-Component. In: Natvig, J.B., et al. Amyloid and Amyloidosis 1990. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-3284-8_221
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DOI: https://doi.org/10.1007/978-94-011-3284-8_221
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