Abstract
1. Lysine-43 (Lys43) in the prosegment region was located within 3 x 10(-1) of catalytic sites, Asp81 and Asp266, in a stereo structure model of rat prorenin. 2. A mutant prorenin, Lys43Leu, was produced to elucidate a role of Lys43 in the inactivation of prorenin. Lys43Leu as well as the wild type were inactive at a neutral pH, and activated at an acidic pH. Its acid-activation speed was three times higher than that of the wild type. The mutant prorenin was more labile than the wild type at 55 degrees C and a neutral pH. 3. These results indicate that Lys43 forms ionic bonds with Asp81 and Asp266 to inactivate and stabilize prorenin.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
More From: Clinical and experimental pharmacology & physiology. Supplement
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.