Abstract
Calcium transport by the Ca 2+-pumping ATPase in rat duodenal basolateral-enriched membrane vesicles was stimulated by synthetic calbindin-D 9k in a similar fashion to the purified natural protein. In order to elucidate the mechanism of this effect, various synthetic mutant proteins were studied. Proteins with modifications to the N-terminal Ca 2+-binding domain, or to a cluster of negatively-charged surface residues had altered Ca 2+-binding but these changes did not affect the stimulation of vesicular Ca 2+ transport. It appears that these domains are not essential for the interaction between calbindin-D 9k and the intestinal basolateral Ca 2+-pump.
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.
