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To continue, please click on the link below to re-enable yourself as a Premium user.Mouse and Human Serum Amyloid: Differences in Composition and Immunoreactivity.Amyloid diseases have been linked to amyloid P (AP) and its precursor protein, amyloid beta-protein (A beta). The first three residues of the AP sequence are the same (AP) or very similar to that of the N-terminus of A beta, although AP is a longer and more basic protein, but both AP and A beta are made up of a series of homologous hydrophobic segments which share a similar A beta-like sequence. We and others have measured high levels of AP in the sera of patients with the serological disorder, primary amyloidosis (a.k.a. AA amyloidosis), and in transgenic mice with spontaneous amyloid formation. In these diseases, AP forms a variety of insoluble fibrils, which are associated with hematopoietic cell plasma membranes. From our studies, we have developed a method for purification of mouse and human AP. Our studies showed that mouse and human AP are similar in amino acid composition, but that mouse AP has a different amino acid composition from human serum AP. The differences are also apparent when comparing the sera of normal mice and humans. We have also examined the binding of anti-A beta to various AP preparations. We found that mouse AP binds similarly to both mouse and human A beta and that rabbit anti-A beta does not cross-react with mouse AP. In contrast, we found that human AP only binds human A beta and that anti-A beta, but not AP, does not bind to mouse A beta. These results suggest that different epitopes exist on mouse and human AP and that A beta may bind to different sites on mouse and human AP.Q:
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