Titlebook: Amyloidosis; George G. Glenner,Elliott F. Osserman,Dorothea Zuc Book 1986 Plenum Press, New York 1986 Alzheimer‘s disease.Alzheimer′s dise

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Ausführung der mittelbaren Kühlunginduced tolerance in interpreting the results, a phenomenon which might well be a variable in different studies. In fact we found that one of the so called “tolerizing” protocols actually immunized the mice and prevented the development of oral tolerance due to the dietary casein. This raises the in

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Die Arbeitsstoffe der Kaltdampfanlageity resided in a species of apparent molecular weight around 400,000. These findings suggest that AEF depends on a protein component possibly associated with non-protein material. Interestingly preparations of isolated human or murine AA fibrils had the same effect . as AEF.

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Ausführung der künstlichen Eiserzeugungogeneity could be demonstrated in this protein using two-dimensional gel electrophoresis. Immunologic cross-reactivity between SAA from the three species was not found. In contrast to human and horse HDL, mink HDL was found not to contain apoA-II and only minute amounts of apoC proteins. Normal hors

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The Physico-Chemical, Antigenic, and Functional Heterogeneity of Human Serum Amyloid Ad in murine ascitic fluid. Dishes coated with the four human SAA is., human AA, various mammalian and human proteins as well as with serum from 31 pts. with metastatic Ca. and 23 pts. with inflammatory diseases (ID) were reacted with the m. abs. The amount of binding was determined using .I labelled

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Analysis of X-Ray Scattering by Human AA Fibrils Using Secondary Structure Predictions of Human SAA1inter-fibril packing is the source of the Astbury “cross-β” X-ray scattering pattern that has previously been thought to be characteristic of individual AA fibrils. Furthermore, we suggest that the AA molecule is a globular protein, and contains a small, well-ordered β-sheet, probably of only two st

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