By Gal Bitan, David B. Teplow (auth.), Einar M. Sigurdsson (eds.)
A confirmed number of comfortably reproducible recommendations for learning amyloid proteins and their involvement within the etiology, pathogenesis, analysis, and treatment of amyloid ailments. The individuals offer equipment for the coaching of amyloid and its precursors (oligomers and protofibrils), in vitro assays and analytical options for his or her learn, and cellphone tradition versions and assays for the creation of amyloid proteins. extra chapters current quite simply reproducible strategies for amyloid extraction from tissue, its detection in vitro and in vivo, in addition to nontransgenic tools for constructing amyloid mouse versions. The protocols stick to the winning equipment in Molecular Biology™ sequence structure, each one providing step by step laboratory directions, an advent outlining the main at the back of the process, lists of the mandatory apparatus and reagents, and pointers on troubleshooting and fending off recognized pitfalls.
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Extra resources for Amyloid Proteins: Methods and Protocols
33 Walsh, D. , et al. (1997) Amyloid beta-protein fibrillogenesis. Detection of a protofibrillar intermediate. J. Biol. Chem. 272(35), 22364–22372. 34. Walsh, D. , et al. (1999) Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates. J. Biol. Chem. 274(36), 25945–25952. 34 Lashuel and Grillo-Bosch Purification of Tau 35 4 Purification of Recombinant Tau Protein and Preparation of Alzheimer-Paired Helical Filaments In Vitro Stefan Barghorn, Jacek Biernat, and Eckhard Mandelkow Summary The tau protein is a neuronal microtubule-associated protein.
Neurobiol. Aging 21, S10–S11 (Abstract 48). 15. , and Teplow, D. B. (2001) Amyloid β-protein oligomerization: prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins. J. Biol. Chem. 276, 35176–35184. 16. 16 Fancy, D. A. and Kodadek, T. (1999) Chemistry for the analysis of protein-protein interactions: rapid and efficient cross-linking triggered by long wavelength light. Proc. Natl. Acad. Sci. USA 96, 6020–6024. 17. Fancy, D. , et al. (2000) Scope, limitations and mechanistic aspects of the photo-induced cross-linking of proteins by water-soluble metal complexes.
Apply the clear supernatant onto a cation-exchange chromatography column (see Note 2). 9. Wash out unspecific proteins with 3 to 5 column volumes cation exchange chromatography buffer A until UV-absorption reaches a stable value. 10. Elute the tau protein with a linear gradient of 60% final concentration of cation exchange chromatography buffer B over 6 column volumes and fractionate (see Note 3). Take an aliquot of the eluted fractions containing protein as judged by UV-absorption and analyze for tau protein by SDS-PAGE (see Fig.