Abstract
Abstract It is shown by sedimentation velocity and polarization of fluorescence measurements that yeast enolase in solution becomes more compact on addition of magnesium. This is associated with changes in absorption, fluorescence emission, and fluorescence-polarization spectra, as well as in the thermal stability of the enzyme. Evidence is presented that this structural change is produced by the binding of 1 mole of metal per mole of protein. The dissociation constant, as determined by fluorimetric titrations, is 1.8 ± 0.5 x 10-6 m.
Highlights
It is shown by sedimentation velocity and polarization of fluorescence measurements that yeast enolase in solution becomes more compact on addition of magnesium
Increasing amounts of magnesium added to purified enzyme solution produce proportional increases in activity
This may be Endogenous magnesium remaining as function of time of dialysis
Summary
It is shown by sedimentation velocity and polarization of fluorescence measurements that yeast enolase in solution becomes more compact on addition of magnesium. This is associated with changes in absorption, fluorescence emission, and fluorescence-polarization spectra, as well as in the thermal stability of the enzyme. Evidence is presented that this structural change is produced by the binding of 1 mole of metal per mole of protein. The dissociation constant, as determined by fluorimetric titrations, is 1.8 f 0.5 x 1OV M
Sign-in/Register to view highlights & summary 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.
