Amyloidosis by Nils Eriksen, Earl P. Benditt (auth.), George G. Glenner,

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.)

From a procedure that from the times of Vir chow and Rokitansky, essentially motivated the fairly slim curiosity of pathologists, amyloidosis has risen full-blown as probably the most vital of disorder complexes. Its presence dominat:es the lesions of Alzheimer's illness, a affliction affecting an predicted 2. five million humans within the U. S. A. and thereby heavily rivaling stroke because the 3rd most typical reason behind dying. If, because it has been de­ scribed, Alzheimer's illness is the "Disease of the Century," then amy­ loidosis is the illness advanced of the a while. It impacts in a single or extra of its manifestations each organ of the physique, and is a minimum of as previous because the stricken Egyptian mummies of the pyramids. With an expanding percent of older participants amyloid of the senior inhabitants turns into progressively more common. the topics lined during this Symposium diversity via nearly each scientific scientific distinctiveness. From a regular of 1 paper in all the prior 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, akin to the polyneuropathies and familial Mediterranean fever have additionally prompted ex­ tensive and fascinating investigations that have published the awesome impression of a unmarried amino acid substitution in remodeling a standard protein into. a deadly "amyloidogenic" one.

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17 REFERENCES 1. 2. 3. 4. 5. 6. 7. 8. 9. 10. 11. 12. 13. 14. 15. 16. 17. 18. 19. 20. 21. 22. 23. 24. , Eur. J. , 41, 117 (1974). , Terry, W. , and G1enner, G. , J. Biol. , 247, 5653 (1972). , in: Amyloid and Amyloidosis, (G. G. G1enner, P. P. Costa, and F. ), Excerpta Medica. Amsterdam, Oxford, Princeton, pp. 331 (1980). , and Natvig, J. , Biochem. Biophys. Res. , 69, 19 (1976). Benditt, E. , Hermodsson, M. , and Ericsson, L. , FEBS Letters, 19, 169 (1971). Franklin, E. , FEBS Letters, 22, 121 (1972).

In order to purify the isomers identified by analytical IEF preparative isoelectric focusing was then performed according to Manrique and Lasky [11]. 5% sephadex G-200SF and 3% ampholytes. 2% Comassie Brilliant Blue. 1 M NaCl followed by centrifugation. The amplolytes were then discarded by chromatography in phenyl-Sepharose 4B (Pharmacia). 2. Production of monoclonal antibodies to SAAL and AA. Monoclonal antibodies were produced following a modification [12] of Kohler and Milstein's technique [13].

Protein AA, however, showed a Iowa-potential [16]. Furthermore, from circular dichroism studies and a computer search it was concluded that protein AA contains stretches of amphipatic a-helices [17]. These findings suggest the presence of nona-structures in protein AA amyloid fibrils. To investigate this possibility the molecular conformation of bovine protein AA, reaggregates and fibrils was studied using infrared spectroscopy and X-ray diffraction. MATERIALS AND METHODS Amyloid Fibril Preparations Amyloid fibrils were isolated from the renal papillae of 5 cows with spontaneous AA-amyloidosis [18].

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