Abstract
The interaction between thyroxine hormone and 7 hydroxycoumarin (7HC) was investigated using fluorescence quenching method. The experimental results showed that thyroxine could quench the fluorescence of 7HC by forming the 7HC-thyroxine complex with static quenching. The apparent binding constants (K) between 7HC and thyroxine were determined to be 1.51 x 10(4) (297 K) and 9.06 x 10(3) (310 K). The binding sites (n) 0.98 +/- 0.1. The thermodynamic parameters showed that the interaction between 7HC and thyroxine was driven mainly by hydrogen bonding interactions and van der Waals force. Calibration for thyroxine, based on quenching titration data, was linear in the concentration range 2.0 x 10(-8) to 3.0 x 10(-7) mol/l. The relative standard deviation was 2.58% for 2.0 x 10(-7) mol/l thyroxine (n = 4) and the 3sigma limit of detection was 3.42 x 10(-8) mol/l in cationic surfactant CTAB medium.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
