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

Volumn 493, Issue 2, 2010, Pages 157-168

  Cardinali, Barbara ^a   Profumo, Aldo ^a   Aprile, Anna ^a   Byron, Olwyn ^b   Morris, Gordon ^c   Harding, Stephen E ^c   Stafford, Walter F ^d   Rocco, Mattia ^a  

^a UNIVERSITY OF GENOA   (Italy)

^b UNIVERSITY OF GLASGOW   (United Kingdom)

^c UNIVERSITY OF NOTTINGHAM   (United Kingdom)

^d BOSTON BIOMEDICAL RESEARCH INSTITUTE   (United States)

Author keywords

Analytical ultracentrifugation; Blood coagulation; Differential pressure viscometry; Fibrinogen degradation products; Light scattering; Plasma proteins

Indexed keywords

FIBRINOGEN; HUMAN FIBRINOGEN FRAGMENT X; PLASMIN; UNCLASSIFIED DRUG;

ALPHA CHAIN; ARTICLE; CARBOXY TERMINAL SEQUENCE; CHICKEN; CONTROLLED STUDY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HUMAN; HYDRODYNAMICS; LIGHT SCATTERING; 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; MASS SPECTROMETRY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SPECIES SPECIFICITY;

EID: 72949124019     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2009.10.008     Document Type: Article

References (68)

1. Doolittle R.F. The molecular biology of fibrin. In: Stamatoyannopoulos G., Majerus P.W., Perlmutter R.M., and Varmus H. (Eds). The Molecular Basis of Blood Diseases. third ed. (2000), Saunders, Philadelphia 719-739
2. Blombäck B. Thromb. Res. 83 (1996) 1-75
3. Doolittle R.F. Annu. Rev. Biochem. 53 (1984) 195-229
4. Weisel J.W. Adv. Protein Chem. 70 (2005) 247-299
5. Doolittle R.F., Goldbaum D.M., and Doolittle L.R. J. Mol. Biol. 120 (1978) 311-325
6. Spraggon G., Everse S.J., and Doolittle R.F. Nature 389 (1997) 455-462
7. Yang Z., Kollman J.M., Pandi L., and Doolittle R.F. Biochemistry 40 (2001) 12515-12523
8. Mosesson M.W., Hainfeld J., Wall J., and Haschemeyer R.H. J. Mol. Biol. 153 (1981) 695-718
9. Medved' L.V., Gorkun O.V., and Privalov P.L. FEBS Lett. 160 (1983) 291-295
10. H.P. Erickson, W.E. Fowler, Electron microscopy of fibrinogen, its plasmic fragments and small polymers, in: M.W. Mosesson, R.F. Doolittle (Eds.), Molecular Biology of Fibrinogen and Fibrin, Annals of the New York Academy of Sciences, vol. 408, New York Academy of Sciences, New York, 1983, pp. 146-163.
11. Weisel J.W., Stauffacher C.V., Bullit T.E., and Cohen C. Science 230 (1985) 1388-1391
12. Veklich Y.I., Gorkun O.V., Medved L.V., Nieuwenhuizen W., and Weisel J.W. J. Biol. Chem. 268 (1993) 13577-13585
13. Litvinov R.I., Yakovlev S., Tsurupa G., Gorkun O.V., Medved L., and Weisel J.W. Biochemistry 46 (2007) 9133-9142
14. Doolittle R.F., Watt K.W.K., Cottrell B.A., Strong D.D., and Riley M. Nature 280 (1979) 464-468
15. Crabtree G.R., Comeau C.M., Fowlkes D.M., Fornace Jr. A.J., Malley J.D., and Kant J.A. J. Mol. Biol. 185 (1985) 1-19
16. Rixon M.W., Chan W.-Y., Davie E.W., and Chung D.W. Biochemistry 22 (1983) 3237-3244
17. Sobel J.H., Thibodeau C.A., Kolks M.A., and Canfield R.E. Biochemistry 29 (1990) 8907-8916
18. Weissbach L., and Grieninger G. Proc. Natl. Acad. Sci. USA 87 (1990) 5198-5202
19. Murakawa M., Okamura T., Kamura T., Shibuya T., Harada M., and Niho Y. Thromb. Haemost. 69 (1993) 351-360
20. M. Murakawa, UniProtKB/Swiss-Prot entry P02672, Nucleotide Sequence [genomic DNA] of bovine fibrinogen alpha chain 174-577, submitted (Sep-1998) to the EMBL/GenBank/DDBJ databases.
21. A. Henschen, F. Lottspeich, M. Kehl, C. Southan, Covalent structure of fibrinogen, in: M.W. Mosesson, R.F. Doolittle (Eds.), Molecular Biology of Fibrinogen and Fibrin, Annals of the New York Academy of Sciences, vol. 408, New York Academy of Sciences, New York, 1983, pp. 28-43.
22. Poirot O., O'Toole E., and Notredame C. Nucleic Acids Res. 31 (2003) 3503-3506
23. Cole C., Barber J.D., and Barton G.J. Nucleic Acids Res. 36 Web Server issue (2008) W197-W201
24. Chung D.W., Que B.G., Rixon M.W., Mace Jr. M., and Davie E.W. Biochemistry 22 (1983) 3244-3250
25. Rixon M.W., Chung D.W., and Davie E.W. Biochemistry 24 (1985) 2077-2086
26. Marder V.J., Shulman N.R., and Carroll W.R. J. Biol. Chem. 244 (1969) 2111-2119
27. Takagi T., and Doolittle R.F. Biochemistry 14 (1975) 940-946
28. Mosesson M.W., and Sherry S. Biochemistry 5 (1966) 2829-2835
29. Yee V.C., Pratt K.P., Cote H.C.F., Letrong I., Chung D.W., Davie E.W., Stenkamp R.E., and Teller D.C. Structure 5 (1997) 125-138
30. Brown J.H., Volkmann N., Jun G., Henschen-Edman A.H., and Cohen C. Proc. Natl. Acad. Sci. USA 97 (2000) 85-90
31. Madrazo J., Brown J.H., Litvinovich S., Dominguez R., Yakovlev S., Medved L., and Cohen C. Proc. Natl. Acad. Sci. USA 98 (2001) 11967-11972
32. Pechik I., Madrazo J., Mosesson M.W., Hernandez I., Gilliland G.L., and Medved L. Proc. Natl. Acad. Sci. USA 101 (2004) 2718-2723
33. Kostelansky M.S., Bolliger-Stucki B., Betts L., Gorkun O.V., and Lord S.T. Biochemistry 43 (2004) 2465-2474
34. Doolittle R.F. J. Thromb. Haemost. 2 (2004) 683-689
35. Kollman J.M., Pandi L., Sawaya M.R., Riley M., and Doolittle R.F. Biochemistry 48 (2009) 3877-3886
36. Tsurupa G., Tsonev L., and Medved L. Biochemistry 41 (2002) 6449-6459
37. Burton R.A., Tsurupa G., Medved L., and Tjandra N. Biochemistry 45 (2006) 2257-2266
38. Burton R.A., Tsurupa G., Hantgan R.R., Tjandra N., and Medved L. Biochemistry 46 (2007) 8550-8560
39. Mihalyi E. Biochemistry 7 (1968) 208-223
40. Spotorno B., Piccinini L., Tassara G., Ruggiero C., Nardini M., Molina F., and Rocco M. Eur. Biophys. J. 25 (1997) 373-384 (Erratum 26 (1997) 417)
41. Laemmli U.K. Nature 227 (1970) 680-685
42. Koppert P.W., Huijsmans C.M.G., and Nieuwenhuizen W. Blood 66 (1985) 503-507
43. Odrljin T.M., Rybarczyk B.J., Francis C.W., Lawrence S.O., Hamaguchi M., and Simpson-Haidaris P.J. Biochim. Biophys. Acta 1298 (1996) 69-77
44. Profumo A., Turci M., Damonte G., Ferri F., Magatti D., Cardinali B., Cuniberti C., and Rocco M. Biochemistry 42 (2003) 12335-12348
45. Van Ruijven-Vermeer I.A., and Nieuwenhuinzen W. Biochem. J. 169 (1978) 653-658
46. Holm B., Nilsen D.W.T., Kierulf P., and Godal H. Thromb. Res. 37 (1985) 165-176
47. Ramarao C.S., and Garbers D.L. J. Biol. Chem. 263 (1988) 1524-1529
48. Stafford W.F. Analytical Ultracentrifugation. Sedimentation Velocity Analysis, Current Protocols in Protein Science. 20.7.1-20.7.11 (2003), John Wiley & Sons, New York
49. Harding S.E. Analysis of polysaccharide size, shape and interactions. In: Scott D.J., Harding S.E., and Rowe A.J. (Eds). Analytical Ultracentrifugation Techniques and Methods (2005), Royal Society of Chemistry, Cambridge 231-252
50. Ralston G. Introduction to Analytical Ultracentrifugation (1993), Beckman Instruments Inc., Palo Alto, CA pp 27-28
51. N. Gralén, Sedimentation and Diffusion Measurements on Cellulose and Cellulose Derivatives, PhD Dissertation, University of Uppsala, Sweden, 1944.
52. Rowe A.J. Biopolymers 16 (1977) 2595-2611
53. Stafford W.F., and Sherwood P.J. Biophys. Chem. 108 (2004) 231-243
54. Bernocco S., Ferri F., Profumo A., Cuniberti C., and Rocco M. Biophys. J. 79 (2000) 561-583
55. Perlmann G.E., and Longsworth L.G. J. Am. Chem. Soc. 70 (1948) 2719-2724
56. Schulz G.V., and Ende H.A. Z. Phys. Chem. 36 (1963) 82-96
57. Zhu H., Ownby D.W., Riggs C.K., Nolasco N.J., Stoops J.K., and Riggs A.F. J. Biol. Chem. 271 (1996) 30007-30021
58. McMeekin T.L., Wilensky M., and Groves M.L. Biochem. Biophys. Res. Commun. 7 (1962) 151-156
59. Ball V., and Ramsden J.J. Biopolymers 46 (1998) 489-492
60. E. Mihalyi, Kinetics and molecular mechanism of the proteolytic fragmentation of fibrinogen, in: M.W. Mosesson, R.F. Doolittle (Eds.), Molecular Biology of Fibrinogen and Fibrin, Ann. New York Acad. Sci., vol. 408, 1983, pp. 60-70.
61. Brennan S.O. Thromb. Haemost. 78 (1997) 1055-1058
62. Dietler G., Wiltzius P., Grolimund P., Kanzig W., Haberli A., and Straub P.W. Early plasmin digestion of fibrinogen: light scattering data. Fibrinogen - Structure, Functional Aspects, Metabolism, vol. 2 (1983), Walter de Gruyter & Co., Berlin-New York 19-23
63. Palmer G.R., Fritz O.G., and Hallett F.R. Biopolymers 18 (1979) 1647-1658
64. Mosesson M.W., Alkjaersing N., Sweet B., and Sherry S. Biochemistry 6 (1967) 3279-3287
65. Doolittle R.F. Adv. Prot. Chem. 27 (1973) 1-109
66. Scheraga H.A., and Laskowski Jr. M. Adv. Prot. Chem. 12 (1957) 1-131
67. Lederer K., and Hammel R. Makromol. Chem. 176 (1975) 2619-2639
68. Rocco M., Infusini E., Daga M.G., Gogioso L., and Cuniberti C. EMBO J. 6 (1987) 2343-2349