Abstract
The reassociation process of the urea-denatured allosteric L-lactate dehydrogenase from Lactobacillus casei was investigated by hybridization experiments between the reassociating enzymes from L. casei and Lactobacillus curvatus. The quantitatively evaluated hybridization patterns indicate an assembly pathway from the unfolded subunits to the tetrameric state via dimers. The comparison of the kinetics of reassociation and reactivation of the L. casei L-lactate dehydrogenase shows that the tetramer is the only active form.
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.
