Fibrinogen-β-estradiol binding studied by fluorescence spectroscopy: Denaturation and pH effects

Journal of Fluorescence

Volumn 16, Issue 2, 2006, Pages 207-213

  Gonçalves, Sónia ^a   Santos, Nuno C ^a   Martins Silva, J ^a   Saldanha, Carlota ^a  

^a INSTITUTO DE MEDICINA MOLECULAR   (Portugal)

Author keywords

Binding; Denaturation; Fibrinogen; estradiol; Fluorescence

Indexed keywords

BINDING; DENATURATION; FIBRINOGEN;Β-ESTRADIOL;

CONFORMATIONS; FLUORESCENCE; PH EFFECTS; PROTEINS; SPECTROSCOPIC ANALYSIS;

NITROGEN COMPOUNDS;

ESTRADIOL; FIBRINOGEN; GUANIDINE; TRYPTOPHAN;

BINDING SITE; CHEMISTRY; CONFERENCE PAPER; HUMAN; PH; PROTEIN CONFORMATION; PROTEIN DENATURATION; SPECTROFLUOROMETRY;

BINDING SITES; ESTRADIOL; FIBRINOGEN; GUANIDINE; HUMANS; HYDROGEN-ION CONCENTRATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; SPECTROMETRY, FLUORESCENCE; TRYPTOPHAN;

EID: 33646711479     PISSN: 10530509     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10895-005-0051-y     Document Type: Conference Paper

References (18)

1. A. D. Smith (2004). Oxford Dictionary of Biochemistry and Molecular Biology, Rev. edn., Oxford University Press, Oxford.
2. Y. Veklich, E. K. Ang, L. Lorand, and J. W. Weisel (1998). The complementary aggregation sites if fibrin investigated through examination of polymers of fibrinogen with fragment E. Proc. Natl. Acad. Sci. USA 95, 1438-1442.
3. NCBI Protein Database; http://www.ncbi.nlm.nih.gov/entrez, accessed on October 2005.
4. D. Lominadze and L. W. Dean (2002). Involvement of fibrinogen specific binding in erythrocyte aggregation. FEBS Lett. 517, 41-44.
5. T. Jensen, S. Halvorsen, H. Godal, P. M. Sandset, and O. Skjønsberg (2004). The viscosity of fibrinogen subtractions and of EDTA denatured fibrinogen do not differ from that of native fibrinogen. Thromb. Res. 113, 51-56.
6. J. M. Montejo, K. R. Naqvi, M. P. Lillo, J. González-Rodriguez, and A. U. Acuña (1992). Conformation of human fibrinogen in solution from polarized triplet spectroscopy. Biochemistry 31, 7580-7586.
7. I. Gonçalves, C. Saldanha, and J. Martins-Silva (2001). β-estradiol effect on erythrocyte aggregation - A controlled in vitro study. Clin. Hemorheol. Microcirc. 25, 127-134.
8. M. Prokopowicz, J. Lukasiak, B. Banecki, and A. Przyjazny (2005). In vitro measurement of conformational stability of fibrinogen adsorbed on siloxane. Biomacromolecules 6, 39-45.
9. S. Gonçalves, N. C. Santos, J. Martins-Silva, and C. Saldanha (2006). Fluorescence spectroscopy evaluation of fibrinogen-β-estradiol binding. Submitted.
10. http://www.agsci.ubc.ca/courses/fnh/410protein/1_54.htm, accessed on October 2005.
11. Y. Tanaka, K. Tsumo, M. Umetsu, T. Nakanishi, Y. Yasutake, N. Sakai, M. Yao, I. Tanaka, T. Arakawa, and I. Kumagai (2004). Structural evidence for guanidine-protein side chain interactions: Crystal structure of CutA from Pyrococcus horikoshii in 3 M guanidine hydrochloride. Biochem. Biophys. Res. Commun. 323, 185-191.
12. U. Haddeland, A. Bennick, and F. Brosstad (1995). Stimulating effect on tissue-type plasminogen activator - A new and sensitive indicator of denatured fibrinogen. Thromb. Res. 77, 329-336.
13. C. H. Ramos (2004). A spectroscopic-based laboratory experiment for protein conformational studies. Biochem. Mol. Biol. Educ. 32, 31-34.
14. A. L. Fink, L. J. Calciano, Y. Goto, T. Kurotsu, and D. R. Palleros (1994). Classification of acid denaturation of proteins: Intermediates and unfolded state. Biochemistry 33, 12504-12511.
15. D. K. Debnath, K. Mukhopadhyay, and S. Basak (2005). Acid-induced denaturation and refolding of prothrombin. Biophys. Chem. 116, 159-165.
16. R. Khodarahmi and R. Yazdanparast (2005). Suppression effect of guanidine hydrochloride on α-cyclodextrin-assisted refolding of denatured α-amylase. Process Biochem. 40, 2973-2979.
17. O. B. Ptitsyn, R. H. Pain, G. V. Semisotnov, E. Zerovnik, and O. I. Razgulyaev (1990). Evidence for a molten globule state as a general intermediate in protein folding. FEBS Lett. 262, 20-24.
18. D. T. Haynie and E. Freire (2004). Structural energetics of the molten globule state. Proteins 16, 115-140.