Nils Eriksen, Earl P. Benditt (auth.), George G. Glenner,'s Amyloidosis PDF

By Nils Eriksen, Earl P. Benditt (auth.), George G. Glenner, Elliott F. Osserman, Earl P. Benditt, Evan Calkins, Alan S. Cohen, Dorothea Zucker-Franklin (eds.)

ISBN-10: 1461292921

ISBN-13: 9781461292920

ISBN-10: 1461321999

ISBN-13: 9781461321996

From a strategy that from the times of Vir chow and Rokitansky, essentially influenced the really slim curiosity of pathologists, amyloidosis has risen full-blown as essentially the most very important of affliction complexes. Its presence dominat:es the lesions of Alzheimer's disorder, a illness affecting an envisioned 2. five million humans within the U. S. A. and thereby heavily rivaling stroke because the 3rd most typical reason for demise. If, because it has been de­ scribed, Alzheimer's ailment is the "Disease of the Century," then amy­ loidosis is the ailment complicated of the a long time. It impacts in a single or extra of its manifestations each organ of the physique, and is no less than as previous because the stricken Egyptian mummies of the pyramids. With an expanding percent of older members amyloid of the senior inhabitants turns into more and more widespread. the topics lined during this Symposium diversity via virtually each scientific clinical uniqueness. From a regular of 1 paper in all the previous 3 Symposiums, the explosive curiosity in cerebral amyloidosis has ended in the presentation of 12 papers in this topic within the current quantity. The genetically predisposed familial amyloidotic procedures, comparable to the polyneuropathies and familial Mediterranean fever have additionally influenced ex­ tensive and exciting investigations that have printed the remarkable influence of a unmarried amino acid substitution in reworking a regular protein into. a deadly "amyloidogenic" one.

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247, 5653 (1972). M. Levin, E. C. Franklin, B. Frangione, and M. Pras, J. Clin. , 51, 2773 (1972). A. Zuckerberg, J. Gazith, A. Rimon, T. Reshef, and J. Gafni, Eur. J. , 28, 161 (1972). M. Pras and T. Reshef, Biochim. Biophys. Acta, 271, 193 (1972). P. Westermark, K. Sletten, and M. Eriksson, Lab. , 41, 427 (1979). H. M. Falck, T. Tonroth, and o. Wegelius, Clin. , 19, 137 (1983). M. Pras, M. Schubert, D. Zucker-Franklin, A. Rimon, and E. C. Franklin, J. Clin. , 47, 924 (1968). P. Westermark, Biochim.

R. S. (C. R. Tribe and P. A. ), John Wright and Sons, Bristol (1983), pp. 124-127. H. M. Falck, T. Tornroth, B. Skrifvars, and O. Wege1ius, Acta Med. , 205, 651 (1979). c. R. Tribe, P. A. Bacon, and J. C. S. (C. R. Tribe and P. A. ), John Wright and Sons, Bristol (1983), pp. 183-186. ACKNOWLEDGEMENTS Supported by the Swedish Medical Research Council (Project No. 5941) and the Research Fund of King Gustaf V. 26 THE PHYSICO-CHEMICAL, ANTIGENIC, AND FUNCTIONAL HETEROGENEITY OF HUMAN SERUM AMYLOID A M.

J ;! e 8 6 223 · E, ~ 4 4 ~ 2 ~ 2 o ! """"'~_ '2345 12345 Reaction of monoclonal antibodies (m. ) to human SAA and AA with SAA isomers, AA and other proteins. 1) Reaction against (vs) SAA 1 (isomer 1), 2) vs SAA 2 , 3) vs SAA s , 4) vs SAA 4 , 5) vs AA, 6) vs human albumin, 8) vs ovalbumin, 9) vs human IgG, 10, vs A light chain, 11) vs k light chain, 12) vs no antigen. 5). 2. Production of monoclonal antibodies to human SAA and AA. The initial fusion of SAAL immunized spleen cells resulted in 18 immunoglobulin secreting, transferable clones, five of which were selected (due to better antibody titers) and innoculated in the peritoneal cavity of BALB/c mice resulting in the production of antibody rich ascitic fluid (m.

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Amyloidosis by Nils Eriksen, Earl P. Benditt (auth.), George G. Glenner, Elliott F. Osserman, Earl P. Benditt, Evan Calkins, Alan S. Cohen, Dorothea Zucker-Franklin (eds.)


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