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Tytuł oryginału: Egg yolk platelet proteins from "Xenopus laevis" are amyloidogenic.
Autorzy: Zemanek Grzegorz, Konieczny Leszek, Piekarska Barbara, Rybarska Janina, Stopa Barbara, Spólnik Paweł, Urbanowicz Barbara, Nowak Mateusz, Król Marcin, Roterman Irena
Źródło: Folia Histochem. Cytobiol. 2002: 40 (3) s.311-318, il., bibliogr. 39 poz.
Sygnatura GBL: 304,846

Typ dokumentu:
  • praca doświadczalna
  • tytuł obcojęzyczny

    Wskaźnik treści:
  • zwierzęta

    Streszczenie angielskie: The association of amphibian (Xenopus laevis) egg yolk platelet proteins, represented predominantly by lipovitellin, was studied as a model of the formation of amyloid deposits. Two kinds of molecular organization formed by this protein material - native and heat-denatured - were found to exhibit amyloid properties, although they differ significantly in structural organization. The first consisted in protein molecules arranged in the natural, physiological, net-like platelet organization, with a tendency to orient uni-directionally. The second was obtained by the gradual removal of Congo red from lipovitellin denatured by heating in an excess of dye. This procedure produced twisted fibrillar organization of molecules typical for amyloids, represented predodminantly by end-to-end associated major polypeptide chains of lipovitallin. Both native and denatured structural forms bind Congo red and produce a green birefringence effect, confirming the near-parallel alignment of the complexed Congo red molecules. However, a dye (1,4-bis(1-amino-4-sulfonaphtyl-2-azo)phenylene) closely related to Congo red but with a very weak self-assembling tendency appeared inactive when the spectral shift was studied in a cross-polarization systsem, indicating in this way that dye supramolecularity is an extra factor which may determine binding to amyloid proteins and specific spectral effects.

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