Abstract
In the course of studying the isolation of amyloid fibril proteins, the structural protein P-component was identified. In 1965 an antibody was made to a solubilized fraction of amyloid fibrils that were isolated by a technique of sucrose gradient centrifugation (1). The antibody cross reacted with a circulating plasma alpha globulin and was called P (plasma) component. This plasma component was isolated from amyloid rich tissues from patients with primary (AL) and secondary (AA) types of amyloidosis and identified as a pentagonally structured protein separate from the amyloid fibrils (2,3). Subsequent studies have shown that AP can be extracted uniquely from amyloid tissue and is identical with normal α-1-glycoprotein (4,5). Thus, AP has been the term used for the P-component associated with amyloid tissues and SAP for the P-component found in serum (6). The two proteins are believed to be completely identical and the terms AP and SAP simply denote the site from which P-component has been isolated. AP has been found associated with amyloid fibrils in primary AL (immunoglobulin light chain), secondary AA, and heredofamilial AF (prealbumin) forms of systemic amyloid disease. In addition, it has been found on all deposits of the various localized forms of amyloid with the possible exception of the intracerebral amyloid plaques and neurofibrillary tangles associated with Alzheimer’s disease (7).
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© 1986 Martinus Nijhoff Publishers, Dordrecht
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Skinner, M., Shirahama, T., Cohen, A.S. (1986). Amyloid P-Component: Clinical Implications. In: Marrink, J., Van Rijswijk, M.H. (eds) Amyloidosis. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-4309-4_10
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DOI: https://doi.org/10.1007/978-94-009-4309-4_10
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