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

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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

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Abstract

The shape and solution properties of fibrinogen are affected by the location of the C-terminal portion of the AÎ± 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 AÎ± chains beyond residue AÎ±200. Â© 2009 Elsevier Inc. All rights reserved.

Item Type:	Article
Uncontrolled Keywords:	Analytical ultracentrifugation Blood coagulation Differential pressure viscometry Fibrinogen degradation products Light scattering Plasma proteins fibrinogen human fibrinogen fragment X plasmin unclassified drug alpha chain article carboxy terminal sequence chicken controlled study high performance liquid chromatography human hydrodynamics mass spectrometry molecular weight nonhuman polyacrylamide gel electrophoresis priority journal protein conformation protein determination ultracentrifugation viscometry Western blotting Animals Chickens Fibrin Fibrinogen Degradation Products Fibrinolysin Humans Protein Structure, Secondary Protein Structure, Tertiary Species Specificity
Subjects:	Q Science > QD Chemistry
Schools:	School of Applied Sciences
Related URLs:	Author
References:	Cited By (since 1996): 1 Export Date: 12 May 2011 Source: Scopus CODEN: ABBIA doi: 10.1016/j.abb.2009.10.008 PubMed ID: 19853574 Language of Original Document: English Correspondence Address: Rocco, M.; Biopolimeri e Proteomica, Istituto Nazionale per la Ricerca sul Cancro (IST), Largo R. Benzi 10, I-16132 Genova, Italy; email: mattia.rocco@istge.it Chemicals/CAS: fibrinogen, 9001-32-5; plasmin, 9001-90-5, 9004-09-5; Fibrin Fibrinogen Degradation Products; Fibrinolysin, 3.4.21.7; fibrinogen fragment X References: Doolittle, R.F., The molecular biology of fibrin (2000) The Molecular Basis of Blood Diseases. third ed., pp. 719-739. , Stamatoyannopoulos G., Majerus P.W., Perlmutter R.M., and Varmus H. (Eds), Saunders, Philadelphia; BlombÃ¤ck, B., (1996) Thromb. Res., 83, pp. 1-75; Doolittle, R.F., (1984) Annu. Rev. Biochem., 53, pp. 195-229; Weisel, J.W., (2005) Adv. Protein Chem., 70, pp. 247-299; Doolittle, R.F., Goldbaum, D.M., Doolittle, L.R., (1978) J. Mol. 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Depositing User:	Gordon Morris
Date Deposited:	19 May 2011 12:08
Last Modified:	19 May 2011 12:08
URI:	http://eprints.hud.ac.uk/id/eprint/10462

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