Abstract
SummaryA cyclic AMP-dependent protein kinase was partially purified from toad urinary bladder epithelium. Cyclic AMP-stimulated protein kinase activity as well as the unstimulated (control) activity of the enzyme was maximal at pH 6.5 using Tris-maleate, sodium cacodylate or sodium acetate buffers. The apparent Km value of cyclic AMP for the stimulation of the enzyme (in sodium acetate buffer and in the presence of 10 mM Mg2+) was 1.5 × 10-9M. The acyclic nucleotide 5'-AMP (in the concentration range 5 × 10-10 to 5 × 10-5M) failed to activate bladder protein kinase. Ca2+ was found to be inhibitory at concentrations higher than 5 × 10-4M. A role for cyclic AMP-dependent protein kinase in neurohypophyseal hormone-induced permeability changes is discussed.
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: Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.)
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.
