Abstract
PRECISE analyses of human amyloid laden tissues have shown that they contain at least two specific components—a fibrillar protein of uniform cross-sectional diameter1,2 and a rod-shaped protein (P-component). Units of the latter look pentagonal under the electron microscope and show antigenic identity with an α-globulin present in human plasma3–5. Preliminary studies have also suggested that the fibrillar component of amyloid is non-immunogenic whereas the P-component is capable of eliciting a strong antibody response6–8. Recently, we have succeeded in preparing antisera not only to the P-component but also to alkali degraded amyloid fibrils (DAM), according to the method of Pras et al.9. Here we show that these antisera react not only with DAM but also with amyloid deposits in various tissues, particularly liver, spleen and kidney. Data are also presented which compare the tissue reactivity of anti-DAM and anti-P-component antisera measured by the fluorescent antibody technique.
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CATHCART, E., SKINNER, M., COHEN, A. et al. Antigenic Determinants in Amyloid Deposits. Nature 228, 1090–1091 (1970). https://doi.org/10.1038/2281090b0
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DOI: https://doi.org/10.1038/2281090b0
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