Abstract
The effect of guanidine chloride on the activity of bovine heart lactate dehydrogenase transferred to a system that was made with toluene, phospholipids, Triton X-100 and 3.8 % water ( v v ) was studied. The activity of the enzyme in the latter system was about 30 times lower than in standard water mixtues. In the low water system, 1.5 and 2.0 M guanidine chloride increased the activity by approximately 20 times. These concentrations of guanidine chloride caused complete inactivation of the enzyme in conventional water systems. The activating effect of the denaturant was independent of enzyme concentration. It is suggested that the increase in activity produced by guanidine chloride was due to a facilitation of the protein-solvent interactions that operate in a catalytic cycle.
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.
