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Search for: [Abstract = "activator inhibitor 1 concentration, fibrinogen concentration, sex and body\-mass index. Increased α2\-antiplasmin incorporation into the clot \(top quartile\) was associated with higher peak thrombin and endogenous thrombin potential. In the next step, the post\-translational modifications of fibrinogen were investigated with mass\-spectrometry in plasma fibrin clots of diabetic patients before and after introducing the treatment with acetylsalicylic acid at the dose of 75 mg once daily. The administration of acetylsalicylic acid was confirmed by suppressed level of thromboxane B2. There were 10 glycation sites identified in α and β fibrinogen chains, and 6 in γ fibrinogen chain. The lysine residues found to be glycated, were previously reported to be involved in cross\-linking by factor XIII \(αK 208, αK\-448 and αK\-539\) and plasmin cleavage \(αK 81\). There were 7 acetylation sites. Three acetylation sites were identical with FL sites \(αK\-195, β\-247 and βK 353\). Treatment with acetylsalicylic acid did not affect intensity of acetylation, as well as clot lysis time assessed according to Pieters et al. The last investigated factors were post\-translational modifications of α2\-antiplasmin glycated and acetylated in vitro. There were 11 glycation sites and 10 acetylation sites. Incubation of α2\-antiplasmin with glucose was associated with glycation of 4 \(K\-418, K\-427, K\-434 and K\-44"]

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