Abstract
The binding of NAD + to glyceraldehyde-3-phosphate dehydrogenase ( d-glyceraldehyde-3-phosphate: NAD + oxidoreductase (phosphorylating), EC 1.2.1.12) from rabbit muscle has been studied by the technique of protein fluorescence quenching. The results are consistent with a model in which binding of the fourth molecule of coenzyme causes a quenching of the protein fluorescence, and the dissociation constants we obtain agree well with those derived by other techniques. The results are not consistent with the earlier proposal that the binding of the fourth molecule of coenzyme causes no overall change in protein fluorescence, and reasons for the differences between the conclusions are discussed.
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.
