کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1316079 | 976421 | 2010 | 6 صفحه PDF | دانلود رایگان |
In this paper we explore the use of fluorescently labeled cytochrome c peroxidase (CcP) from baker's yeast for monitoring nitric oxide (NO) down to the sub-micromolar level, by means of a FRET (Förster Resonance Energy Transfer) mechanism. The binding affinity constant (Kd) for the NO binding to CcP was determined to be 10 ± 1.5 µM. The rate of NO dissociation from the CcP (koff) and the second order rate constant for the NO association (kon) were found to be 0.22 ± 0.08 min− 1 and 0.024 ± 0.002 µM− 1 min− 1 respectively. The immobilization of fluorescently labeled CcP into a polymeric matrix for use in a solid state NO sensing device was also explored. The results provide proof-of-principle that labeled CcP can be successfully implemented in a fast, simple, quantitative and sensitive NO sensing device.
Figure optionsDownload as PowerPoint slide
Journal: Journal of Inorganic Biochemistry - Volume 104, Issue 6, June 2010, Pages 619–624