Functional consequences of tryptophan modification in human fibrinogen.
When human fibrinogen was modified with H2O2, inter- and intra-molecular cross-links of fibrinogen were formed, accompanied with oxidation of tryptophan, methionine and tyrosine residues. These cross-links may be closely associated with oxidation of tryptophan residues. The polymerization activity of fibrinogen with thrombin was decreased markedly by this modification. Modification of tryptophan residues in fibrinogen was also performed with 2-hydroxy-5-nitrobenzyl bromide. Modification of two out of a total 78 tryptophan residues in the molecule with the reagent led to the intensification (1.7 times) of the polymerization activity with thrombin and further modification of the next two residues led to complete loss of the polymerization activity. The first two tryptophan residues to be modified are in Fragment D, and the next two occur in Fragment E.
D015077:2-Hydroxy-5-nitrobenzyl Bromide; D005340:Fibrinogen / Q000378:metabolism; D006801:Humans; D006861:Hydrogen Peroxide; D010084:Oxidation-Reduction; D011485:Protein Binding; D013053:Spectrophotometry; D013917:Thrombin; D014364:Tryptophan
D015077:2-Hydroxy-5-nitrobenzyl Bromide; D014364:Tryptophan; D005340:Fibrinogen; D006861:Hydrogen Peroxide; D013917:Thrombin