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.
Keywords
Human fibrinogen - Fragment D and E - Intrinsic fluorescence