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 |
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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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