Year-end Sale % OFF 
Abstract
ATP and Mg ++ produced a striking inhibition of Na +-stimulated amino acid and phosphate transport activity assayed in vesicles isolated from the plasma membrane of SV40-transformed and nontransformed mouse fibroblasts. The α-β and β-γ-methylene analogs of ATP were ineffective. Purified membrane vesicles contain an endogenous protein kinase activity which catalyzes autophosphorylation of membrane proteins in the presence of ATP. This provides an experimental approach to investigate the role of membrane protein phosphorylation in mediating permeability changes in response to changes in cellular proliferative or transformed state.
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.
