作者: R. H. Painter , I. De Escallón , A. Massey , L. Pinteric , S. B. Stern
DOI: 10.1111/J.1749-6632.1982.TB22138.X
关键词:
摘要: No difference have been observed in the properties of amyloid P-component (AP) and its serum counterpart (SAP) which might account for deposition former amyloidosis. Purified by nonselective techniques, preparations AP SAP were shown to similar molecular weights peptide composition, identical morphology electron microscope (EM) be antigenically indistinguishable. Both proteins soluble EDTA but readily precipitated presence calcium ions, forming characteristic two-dimensional arrays EM. In however, was not aggregated sedimented at 9.5S Ca2+ as did purified protein EDTA. Precipitation could prevented pretreatment with acid hydrolysates agarose or SP Sephadex, matrices has a calcium-dependent affinity. It is proposed that circulates combination low weight natural ligand prevents aggregation. While identity yet unknown, it likely resemble glycosidic subunits agarose.