Congophilicity (Congo red affinity) of different beta2-microglobulin conformations characterized by dye affinity capillary electrophoresis.

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Congophilicity (Congo red affinity) of different beta2-microglobulin conformations characterized by dye affinity capillary electrophoresis. / Heegaard, N H; Sen, J W; Nissen, Mogens Holst.

In: Journal of Chromatography A, Vol. 894, No. 1-2, 2000, p. 319-27.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Heegaard, NH, Sen, JW & Nissen, MH 2000, 'Congophilicity (Congo red affinity) of different beta2-microglobulin conformations characterized by dye affinity capillary electrophoresis.', Journal of Chromatography A, vol. 894, no. 1-2, pp. 319-27.

APA

Heegaard, N. H., Sen, J. W., & Nissen, M. H. (2000). Congophilicity (Congo red affinity) of different beta2-microglobulin conformations characterized by dye affinity capillary electrophoresis. Journal of Chromatography A, 894(1-2), 319-27.

Vancouver

Heegaard NH, Sen JW, Nissen MH. Congophilicity (Congo red affinity) of different beta2-microglobulin conformations characterized by dye affinity capillary electrophoresis. Journal of Chromatography A. 2000;894(1-2):319-27.

Author

Heegaard, N H ; Sen, J W ; Nissen, Mogens Holst. / Congophilicity (Congo red affinity) of different beta2-microglobulin conformations characterized by dye affinity capillary electrophoresis. In: Journal of Chromatography A. 2000 ; Vol. 894, No. 1-2. pp. 319-27.

Bibtex

@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",

}

RIS

TY - JOUR

T1 - Congophilicity (Congo red affinity) of different beta2-microglobulin conformations characterized by dye affinity capillary electrophoresis.

AU - Heegaard, N H

AU - Sen, J W

AU - Nissen, Mogens Holst

N1 - Keywords: Coloring Agents; Congo Red; Electrophoresis, Capillary; Mass Spectrometry; Protein Conformation; beta 2-Microglobulin

PY - 2000

Y1 - 2000

N2 - 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.

AB - 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.

M3 - Journal article

C2 - 11100875

VL - 894

SP - 319

EP - 327

JO - Journal of Chromatography

JF - Journal of Chromatography

SN - 0301-4770

IS - 1-2

ER -

ID: 8746353