Abstract
The structure of yeast phosphoglyceric acid mutase in phosphate buffer and in urea solutions has been investigated by ultraviolet spectra, optical rotatory dispersion measurements, and ultracentrifugal analyses. The results suggest that the native enzyme may be “nonhelical” and that the conformation is stabilized by hydrophobic forces associated with water as a solvent. Other possibilities have also been discussed. The native enzyme, which has no disulfide linkages, is unfolded and dissociates into subunits at concentrations greater than 2 M urea. Reactivation and reconstitution of the enzyme denatured in 8 M urea by dilution or removal of urea have been observed. Regeneration depends on the pH and on the nature and concentrations of ions in the diluents. Comparison of the physicochemical and enzymic properties has suggested that the reconstituted and native enzymes are identical.
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.
