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Human fibrinogen and its fragment were modified with 2-hydroxy-5-nitrobenzyl bromide(HNBB) or with H2O2-dioxane to see the functional significance of tryptophan residues in the fibrinogen molecule. Tryptophan residues were modified with HNBB in a stepwise manner. Modification of two out of the total 64 tryptophan residues in the molecule did not reduce the polymerization activity with thrombin but further modification of the next two residues led to a complete loss of the polymerization activity. The latter two tryptophan residues modified were in Fragment E and the position may be either Trp 33 or Trp 41 in the a-chain in the fibrinogen molecule.  Fragment D inhibited the association activity of fibrin monomer. This inhibitory effect was lost completely by the modification of approximately six out of the total 21 tryptophan residues in the fragment with H2O2-dioxane. These resul ts indicate the significance of tryptophan residues in Fragments D and E of fibrinogen molecule in fibrin polymer formation.

Significance Of Tryptophan Residues In Fibrinogen In Fibrin Polymer Formation