טוען...
Oxygen binding and nitric oxide dioxygenase activity of cytoglobin are altered to different extents by cysteine modification
Cytoglobin (Cygb), like other members of the globin family, is a nitric oxide (NO) dioxygenase, metabolizing NO in an oxygen (O(2))‐dependent manner. We examined the effect of modification of cysteine sulfhydryl groups of Cygb on its O(2) binding and NO dioxygenase activity. The two cysteine sulfhyd...
שמור ב:
| הוצא לאור ב: | FEBS Open Bio |
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| Main Authors: | , , , , , |
| פורמט: | Artigo |
| שפה: | Inglês |
| יצא לאור: |
John Wiley and Sons Inc.
2017
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| נושאים: | |
| גישה מקוונת: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5458454/ https://ncbi.nlm.nih.gov/pubmed/28593139 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/2211-5463.12230 |
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