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Thromb Haemost 1982; 48(01): 021-023
DOI: 10.1055/s-0038-1657207
DOI: 10.1055/s-0038-1657207
Original Article
The Intrinsic Fluorescence of Human Fibrinogen and Its Fragments D and E
Further Information
Publication History
Received 23 November 1981
Accepted 06 May 1982
Publication Date:
13 July 2018 (online)

Summary
The tryptophan fluorescence of fibrinogen and its final degradation products - fragment D and E - were compared. Fibrinogen and its derivatives exhibit identical emission and excitation spectra. Their fluorescence intensity is influenced to a different extent by pH titration and temperature.
Our studies showed that tryptophan residues of core fragments D and E are much more exposed to quenching effects of acrylamide and ions than intact fibrinogen, which may be caused by conformational changes occurring over the domains during plasmin digestion of fibrinogen molecule.
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References
- 1 Blombäck B, Blombäck M, Henschen A, Hessel B, Iwanaga S, Woods KR. N-terminal disulphide knot of human fibrinogen. Nature 1968; 218: 130-134
- 2 Pizzo SV, Schwartz ML, Hill RL. The effect of plasmin on the subunit structure of human fibrinogen. J Biol Chem 1972; 247: 636-645
- 3 Marder VJ. Immunologic structure of fibrinogen and its degradation products. Theoretical and clinical considerations. In: Laki K. (ed.) Fibrinogen, Marcel Dekker Inc; New York: 1968: 339-357
- 4 Marder VJ, Budzyński AZ. Data for defining fibrinogen and its plasmic degradation products. Thrombos Diathes Haemorrh 1975; 33: 199-207
- 5 Iwanaga S, Wallen P, Grondahl NJ, Henschen A, Blombäck B. On the primary structure of human fibrinogen. Isolation and characterisation of N-terminal fragments from plasmic digests. Eur J Biochem 1969; 8: 189-199
- 6 Haverkate F, Timan G, Nieuwenhuizen W. Anticlotting properties of fragments D from human fibrinogen and fibrin. Eur J Clin Invest 1970; 9: 253-255
- 7 Takagi T, Doolittle RF. The amino acid sequence studies of the a chain of human fibrinogen: Location of four plasmin attack points and a covalent crosslinking site. Biochemistry 1975; 14: 5149-5156
- 8 Harfenist EJ, Canfield RE. Degradation of fibrinogen by plasmin. Isolation of an early cleavage product. Biochemistry 1975; 14: 4110-4117
- 9 Hessel B. On the structure of the COOH-terminal part of the Aa chain of human fibrinogen. Thromb Res 1975; 7: 75-87
- 10 Hall GE, Slayter HS. The fibrinogen molecule: Its size, shape and mode of polimerization. J Biophys Biochem Cytol 1959; 5: 11-15
- 11 Tranqui-Pouit L, Marder VJ, Suscillon M, Budzyński AZ, Hudry-Clargeon G. Electron microscopic studies of plasmin degradation products of fibrinogen. Biochim Biophys Acta 1975; 400: 189-199
- 12 Plow E, Edgington TS. Molecular events responsible for modulation of neoantigenic expressions the cleavage-associated neoantigen of fibrinogen. Proc Natl Acad Sci US 1972; 69: 208-212
- 13 Edgington TS, Plow EF. Conformational and structural modulation of the N-terminal regions of fibrinogen and fibrin associated with plasmin cleavage. J Biol Chem 1975; 250: 3393-3398
- 14 Nilehn JE. Split products of fibrinogen after prolonged interaction with plasmin. Thrombos Diathes Haemorrh 1967; 18: 89-100
- 15 Itzhake RF, Gill DM. A microbiuret method for estimating proteins. Anal Biochem 1964; 9: 4-10
- 16 McDonagh J, Messel H, McDonagh RF, Murano G, Blombäck B. Molecular weight analysis of fibrinogen and fibrin chains by an improved sodium dodecyl sulfate gel electrophoresis method. Biochim Biophys Acta 1972; 257: 135-142
- 17 Lehrer SS. Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysosome by iodide ions. Biochemistry 1971; 10: 3254-3263
- 18 Eftink MR, Ghiron CA. Fluorescence quenching of indole and model micelle systems. J Phys Chem 1976; 80: 486-493
- 19 Eftink MR, Ghiron CA. Exposure of tryptophanyl residues in proteins. Quantitative determination by fluorescence quenching studies. Biochemistry 1976; 15: 672-680
- 20 Middaugh CR, Litman GW. Investigation of the molecular basis for the temperature-dependent insolubility of cryoglobulins. VI. Quenching by acrylamide of the intrinsic tryptophan fluorescence of IgM proteins. Biochim Biophys Acta 1978; 535: 33-43
- 21 Arrio-Dupont M. Fluorescence of amino acids in a pyridoxal phosphate enzyme: Asperate aminotransferase. Eur J Biochem 1978; 91: 369-378
- 22 Kronman MJ, Holmes LG. The fluorescence of native denatured and reduced-denatured proteins. Photochem Photobiol 1971; 14: 113-134
- 23 Koval VG, Shavchenko LI, Shcherbatskaya NV. Dependence of the fibrinogen E-fragment fluorescence spectrum on pH medium. Biophysica (Biofizika) 1980; 25: 583-589
- 24 Nojima H, Ikai A, Noda H. Anomalus fluorescence of yeast-3-phosphoglycerate kinase. Biochim Biophys Acta 1976; 427: 20-27
- 25 Lottspeich F, Henschen A. Amino acid sequence of human fibrin. Preliminary note on the completion of the γ-chain sequence. Hoppe-Seyler’s Z Physiol Chem 1977; 358: 935-938
- 26 Henschen A, Lottspeich F. Amino acid sequence of human fibrin. Preliminary note on the completion of the β-chain sequence. Hoppe-Seyler’s Z Physiol Chem 1977; 358: 1643-1646
- 27 Henschen A, Lottspeich F, Hessel B. Amino acid sequence of human fibrin. Preliminary note on the completion of the intermediate part of the α-chain sequence. Hoppe-Seyler’s Z Physiol Chem 1979; 360: 1951-1956
- 28 Doolittle RF, Watt KWK, Cottrell BA, Strong DD, Riley M. The amino acid sequence of the α-chain of human fibrinogen. Nature 1979; 280: 464-468