| Literature DB >> 25799579 |
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Abstract
Entities:
Year: 2015 PMID: 25799579 PMCID: PMC4370769 DOI: 10.1371/journal.pone.0122177
Source DB: PubMed Journal: PLoS One ISSN: 1932-6203 Impact factor: 3.240
Fig 3Function of antithrombin variants.
Anti-FXa activity of antithrombin proteins secreted to the conditioned medium in presence of heparin. Results are expressed as a percentage of the activity of the S137T variant. Each bar represents the mean ± standard deviation (SD) of two independent experiments performed in duplicate. The differences between mutants were tested by paired t-test (p-value). The “*” indicated differences statistically significant with p<0.05.
Fig 4Scheme of binding of antithrombin and heparin.
Initial rapid equilibrium, K , between antithrombin, AT, and pentasaccharide, H, leads to complex, AT.H, followed by rapid conformational change via k to a high heparin affinity, highly fluorescence complex, AT*.H.