Hydrodynamic and mass spectrometry analysis of nearly-intact human fibrinogen, chicken fibrinogen, and of a substantially monodisperse human fibrinogen fragment X

Cardinali, B., Profumo, A., Aprile, A., Byron, O., Morris, G., Harding, S.E., Stafford, W.F. and Rocco, M. (2010) Hydrodynamic and mass spectrometry analysis of nearly-intact human fibrinogen, chicken fibrinogen, and of a substantially monodisperse human fibrinogen fragment X. Archives of Biochemistry and Biophysics, 493(2), pp. 157-168. (doi:10.1016/j.abb.2009.10.008)

Cardinali, B., Profumo, A., Aprile, A., Byron, O., Morris, G., Harding, S.E., Stafford, W.F. and Rocco, M. (2010) Hydrodynamic and mass spectrometry analysis of nearly-intact human fibrinogen, chicken fibrinogen, and of a substantially monodisperse human fibrinogen fragment X. Archives of Biochemistry and Biophysics, 493(2), pp. 157-168. (doi:10.1016/j.abb.2009.10.008)

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Publisher's URL: http://dx.doi.org/10.1016/j.abb.2009.10.008

Abstract

The shape and solution properties of fibrinogen are affected by the location of the C-terminal portion of the Aα chains, which is presently still controversial. We have measured the hydrodynamic properties of a human fibrinogen fraction with these appendages mostly intact, of chicken fibrinogen, where they lack 11 characteristic 13-amino acids repeats, and of human fragment X, a plasmin early degradation product in which they have been removed. The human fibrinogen/fragment X samples were extensively characterized by SDS–PAGE/Western blotting and mass spectrometry, allowing their composition to be precisely determined. The solution properties of all samples were then investigated by analytical ultracentrifugation and size-exclusion HPLC coupled with multi-angle light scattering and differential pressure viscometry detectors. The measured parameters suggest that the extra repeats have little influence on the overall fibrinogen conformation, while a significant change is brought about by the removal of the C-terminal portion of the Aα chains beyond residue Aα200.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Byron, Professor Olwyn
Authors: Cardinali, B., Profumo, A., Aprile, A., Byron, O., Morris, G., Harding, S.E., Stafford, W.F., and Rocco, M.
Subjects:Q Science > QH Natural history > QH345 Biochemistry
College/School:College of Medical Veterinary and Life Sciences > School of Life Sciences
Journal Name:Archives of Biochemistry and Biophysics
ISSN:0003-9861
ISSN (Online):1096-0384
Published Online:22 October 2009

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