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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...

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發表在:FEBS Open Bio
Main Authors: Zhou, Danlei, Hemann, Craig, Boslett, James, Luo, Aiqin, Zweier, Jay L., Liu, Xiaoping
格式: Artigo
語言:Inglês
出版: John Wiley and Sons Inc. 2017
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在線閱讀: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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