@article{fd901e20ba3011ddae57000ea68e967b,
title = "Congophilicity (Congo red affinity) of different beta2-microglobulin conformations characterized by dye affinity capillary electrophoresis.",
abstract = "The amyloidogenic protein beta-microglobulin was characterized by affinity capillary electrophoresis (CE). CE could separate conformational variants of beta2-microglobulin and with the amyloid-specific dye Congo red as a buffer additive it was possible to measure different Congo red-affinities of native and abnormally folded beta2-microglobulin. We find that native beta2-microglobulin has an intermediate affinity for Congo red at pH 7.3 and that binding involves electrostatic interactions. The conformational variant of beta2-microglobulin that appears in acetonitrile solutions binds Congo red more strongly. Affinity CE using Congo red as a buffer additive is a new, simple, fast, and quantitative micromethod for the characterization of soluble conformational intermediates of amyloidogenic proteins.",
author = "Heegaard, {N H} and Sen, {J W} and Nissen, {Mogens Holst}",
note = "Keywords: Coloring Agents; Congo Red; Electrophoresis, Capillary; Mass Spectrometry; Protein Conformation; beta 2-Microglobulin",
year = "2000",
language = "English",
volume = "894",
pages = "319--27",
journal = "Journal of Chromatography",
issn = "0301-4770",
publisher = "Elsevier",
number = "1-2",
}