Abstract
1. 1. The present study demonstrated that the Ca 2+-ATPase activity of the plasma membrane-rich fraction from bovine parotid gland was decreased by the addition of reducing agents. 2. 2. Ca 2+-ATPase activity staining on SDS-PAGE gels was lost in the presence of 2-mercaptoethanol. 3. 3. Among all the reducing agents tested, GSH was the most effective in inhibiting Ca 2+-ATPase. 4. 4. The Ca 2+-ATPase activity decreased by the GSH was restored by the addition of an oxidizing reagent. However, oxidation with an oxidizing reagent subsequent to alkylation of the reduced enzyme with iodoacetamide resulted in no restoration of activity. 5. 5. The decrease of Ca 2+-ATPase activity by GSH is due to a decrease in the V ax of the enzyme. 6. 6. These results suggest that the disulfide bond in this enzyme protein is necessary to maintain the activity of this enzyme.
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 callMore From: Comparative Biochemistry and Physiology -- Part B: Biochemistry and Molecular Biology
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.
