کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2001848 1066065 2007 9 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Reduction and S-nitrosation of the neuropeptide oxytocin: Implications for its biological function
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Reduction and S-nitrosation of the neuropeptide oxytocin: Implications for its biological function
چکیده انگلیسی

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 1.8 h with respect to reformation of OT disulfide at 37 °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.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Nitric Oxide - Volume 17, Issue 2, September 2007, Pages 82–90
نویسندگان
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