Abstract
Arsenate, an analogue of inorganic phosphate, causes an increase in the intrinsic fluorescence of the Ca 2+-ATPase of sarcoplasmic reticulum membranes. This increase in fluorescence is observed regardless of whether Ca 2+-loaded or leaky vesicles are assayed. The maximal fluorescence change (2–3%) is observed at pH 6.0 in the presence of Mg 2+ and is abolished by the addition of micromolar Ca 2+ concentrations. Dimethyl sulfoxide (20% v v ) increases the enzyme's affinity for arsenate one order of magnitude. It is concluded that arsenate, after binding, promotes the same conformational change of the enzyme as that produced by P i.
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.
