Thromb Haemost 1982; 48(01): 021-023
DOI: 10.1055/s-0038-1657207
Original Article
Schattauer GmbH Stuttgart

The Intrinsic Fluorescence of Human Fibrinogen and Its Fragments D and E

M A Kowalska
The Department of Biophysics, Institute of Physiology and Biochemistry, Medical School in Lódź, Lódź, Poland
,
C S Cierniewski
The Department of Biophysics, Institute of Physiology and Biochemistry, Medical School in Lódź, Lódź, Poland
› Author Affiliations
Further Information

Publication History

Received 23 November 1981

Accepted 06 May 1982

Publication Date:
13 July 2018 (online)

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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.