Year-end Sale % OFF 
Abstract
Using a stopped flow apparatus, the effects of 2,3-diphosphoglycerate (DPG), and pH on the hemoglobin-oxygen dissociation kinetic constants were determined. The order of kinetics was pseudo-first order between 85 and 40% saturation. Increasing the concentration of DPG increased the kinetic constants in a manner which is related to the extent of binding of DPG to hemoglobin. The dependence of the kinetic constants on pH was, however, not explained in terms of the total number of DPG bound to oxyhemoglobin. The DPG was affecting the kinetic constants in such a manner that the binding was functionally linked to the Bohr proton.
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 callMore From: Biochemical and Biophysical Research Communications
Disclaimer: 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.
