Abstract
Homogeneous-type enzyme-linked competitive binding assays utilizing the synthetic enzyme–biotin and avidin–riboflavin conjugates are developed for the detection of riboflavin as well as its binder protein. The activity of the enzyme–biotin conjugate is inhibited in the presence of the avidin–riboflavin conjugate, and the observed inhibition is reversed in an amount dependent on the concentration of riboflavin binding protein (RBP) added. Upon additions of free riboflavin to the mixture, activity is reinhibited in an amount proportional to the riboflavin concentration. Three different enzymes are examined as the labels: glucose-6-phosphate dehydrogenase, adenosine deaminase, and alkaline phosphatase. The catalytic activity of these enzymes, when conjugated with biotin, is shown to be inhibited to a significant degree (>90%) by the binding of the avidin–riboflavin conjugate, and reversed upon additions of RBP.
Sign-in/Register to access full text options 
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.
