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Sci. Signal., 10 November 2009
[DOI: 10.1126/scisignal.2000464]

Supplementary Materials for:

H2S Signals Through Protein S-Sulfhydration

Asif K. Mustafa, Moataz M. Gadalla, Nilkantha Sen, Seyun Kim, Weitong Mu, Sadia K. Gazi, Roxanne K. Barrow, Guangdong Yang, Rui Wang, Solomon H. Snyder*

*To whom correspondence should be addressed. E-mail: ssnyder{at}jhmi.edu

This PDF file includes:

  • Fig. S1. Modified biotin switch assay for protein S-sulfhydration.
  • Fig. S2. The non–PLP-binding CSE mutant is catalytically inactive.
  • Fig. S3. The modified biotin switch assay is specific for sulfhydration.
  • Fig. S4. L-Cysteine levels are comparable in wild-type and CSE/ livers.
  • Fig. S5. Wild-type and CBS/ livers show similar H2S production.
  • Fig. S6. GAPDH is substantially sulfhydrated during cell-free catalysis by CSE and L-cysteine.
  • Fig. S7. GAPDH sulfhydration at Cys150 with LC-MS/MS.
  • Fig. S8. H2S sulfhydrates ATP-sensitive potassium channels in HEK293 cells.

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Technical Details

Format: Adobe Acrobat PDF

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A. K. Mustafa, M. M. Gadalla, N. Sen, S. Kim, W. Mu, S. K. Gazi, R. K. Barrow, G. Yang, R. Wang, S. H. Snyder, H2S signals through protein S-sulfhydration. Sci. Signal. 2, ra72 (2009).

© 2009 American Association for the Advancement of Science


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