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Fig. 5 The VWF A2 domain exists predominantly in a reduced dithiol and glutathionylated form in healthy donors. The VWF A2 domain exists predominantly.

Published byIngvar Brodersen Modified over 5 years ago

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Presentation on theme: "Fig. 5 The VWF A2 domain exists predominantly in a reduced dithiol and glutathionylated form in healthy donors. The VWF A2 domain exists predominantly."— Presentation transcript:

1 Fig. 5 The VWF A2 domain exists predominantly in a reduced dithiol and glutathionylated form in healthy donors. The VWF A2 domain exists predominantly in a reduced dithiol and glutathionylated form in healthy donors. (A) Distribution of reduced, glutathionylated, and oxidized VWF A2 in 22 healthy donor plasmas. Mean and range for the two A2 domain cysteine-containing peptides of individual samples are shown on the left, and the mean and SD for the 22 samples are shown on the right. The VWF A2 domain cysteine pair exists as unpaired thiols in ~40%, Cys1669 exists as an unpaired thiol and Cys1670 is glutathionylated in ~36%, and the pair exists in an oxidized disulfide form in ~24%. (B) Posttranslational modifications of the A2 domain cysteines. (C) Distribution of unmodified and oxidized Met1606 in the 22 healthy donor plasmas. The mean and SD for the 22 samples are shown on the right. Only a minor fraction of VWF Met1606 is oxidized in the cohort of healthy donors. Diego Butera et al. Sci Adv 2018;4:eaaq1477 Copyright © 2018 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC).

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