Fig. 4: Prevention of disulfide bond formation during fibrin formation alters the polymer structure.
From: Fibrinogen function achieved through multiple covalent states
a Purified fibrinogen (Fbg) was treated with 12C-IPA (Fbg-IPA) to block the unpaired cysteine thiols in the protein. Labeling conditions were identical to that for the mass spectrometry experiments (Figs. 1–5). b Alkylation of the unpaired cysteine thiols in fibrinogen with IPA does not impair the fibrin forming capacity of the protein. The data points are the mean ± SD from three independent experiments and represent the percentage of Fbg/Fbg-IPA consumed in the formation of fibrin polymer. Source data are provided as a Source Data file. c Kinetics of fibrin polymerization from Fbg and Fbg-IPA measured by light scattering. The data points are the mean ± SD from three independent experiments. Source data are provided as a Source Data file. d Representative structures from n = 20 images of fibrin matrices from Fbg and Fbg-IPA characterized by scanning electron microscopy.
