Abstract
Similar distributions of radioactivity were observed upon paper electrophoresis of pepsin-digested beef brain microsomes previously exposed to either [ 32P]ATP or acetyl [ 32P]phosphate in the presence of Na + and Mg 2+. ATP and acetylphosphate were each competitive inhibitors of the other as substrate for a K +-requiring acetylphosphate (acylphosphate phosphohydrolase, EC 3.6.1.7) and for a (Na + + K +)-dependent ATPase (ATP phosphohydrolase, EC 3.6.1.3). Despite these similarities, there were marked differences in the inhibitory effect of ouabain, oligomycin, and exposure to N-ethylmaleimide on the two enzymes. The data suggest that the K +-acetyl-phosphatase activity of the beef brain may represent a different entity than the ( Na + + K +)-ATPase.
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.
