Cardinali, B., Profumo, A., Aprile, A., Byron, O., Morris, Gordon, 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. ISSN 0003-9861

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. © 2009 Elsevier Inc. All rights reserved.

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