| Keyword search (4,163 papers available) | ![]() |
Concordia Publications:
| Title | Authors | PubMed ID | |
|---|---|---|---|
| 1 | Characterization of Phase I and Glucuronide Phase II Metabolites of 17 Mycotoxins Using Liquid Chromatography-High-Resolution Mass Spectrometry | Slobodchikova I; Sivakumar R; Rahman MS; Vuckovic D; | 31344861 CBAMS |
| 2 | Evaluation of D10-Leu metabolic labeling coupled with MALDI-MS analysis in studying the response of the yeast proteome to H2O2 challenge | Jiang H; English AM; | 17022625 CBAMS |
| 3 | Reduction and S-nitrosation of the neuropeptide oxytocin: implications for its biological function | Roy JF; Chrétien MN; Woodside B; English AM; | 17692543 CBAMS |
| 4 | Human blood cell levels of 5-hydroxymethylcytosine (5hmC) decline with age, partly related to acquired mutations in TET2 | Buscarlet M; Tessier A; Provost S; Mollica L; Busque L; | 27475703 CBAMS |
| Title: | Reduction and S-nitrosation of the neuropeptide oxytocin: implications for its biological function | ||||
| Authors: | Roy JF, Chrétien MN, Woodside B, English AM | ||||
| Link: | https://pubmed.ncbi.nlm.nih.gov/17692543/ | ||||
| DOI: | 10.1016/j.niox.2007.06.005 | ||||
| Publication: | Nitric oxide : biology and chemistry | ||||
| Keywords: | |||||
| PMID: | 17692543 | Category: | Nitric Oxide | Date Added: | 2019-06-19 |
| Dept Affiliation: |
CBAMS
1 Department of Chemistry and Biochemistry, Centre for Biological Applications of Mass Spectrometry, Concordia University, 7141 Sherbrooke Street W., Montreal, Que., Canada. |
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Description: |
Oxytocin (OT; Cys-Tyr-Ile-Gln-Asn-Cys-Pro-leu-Gly), a posterior pituitary peptide hormone, is characterized by a Cys1-Cys6 disulfide bond in its stable, isolated state. This paper describes a simple, one-step method for the production of OT in its reduced, dithiol form (OT dithiol), free of reducing agent. The effects of temperature, pH, and metal-ion chelators on the autoxidation of OT dithiol were examined to establish if this form is likely to persist under biological conditions. It was found that OT dithiol has a half-life of 1.8h with respect to reformation of OT disulfide at 37 degrees C and pH 6.9 in the presence of the copper chelators, DTPA and neocuproine. S-Nitrosation of OT dithiol by acidified nitrite at pH 3.0 was examined by absorption spectroscopy and HPLC-UV-MS, which revealed that both singly and doubly S-nitrosated OT are formed. These results suggest novel chemical aspects to OT signaling, the biological implications of which are discussed here. |



