Characterization of [125I]endothelin-1 binding sites in rat cardiac membrane fragments.


Standard binding and displacement techniques were used to identify high-affinity binding sites for [125I]-labeled endothelin-1 (ET-1) in membranes harvested from the hearts of adult female Sprague-Dawley rats. A single population of binding sites was identified, with a KD of 0.20 +/- 0.03 nM at 37 degrees C, and a Bmax of 93.5 +/- 6.4 fmol/mg protein. Bound… (More)


Figures and Tables

Sorry, we couldn't extract any figures or tables for this paper.

Slides referencing similar topics