Abstract:
:High affinity Ins(1,4,5)P3-binding sites of permeabilized hepatocytes are probably the ligand recognition sites of the receptors that mediate the effects of Ins(1,4,5)P3 on intracellular Ca2+ mobilization. We have now solubilized these sites from rat liver membranes in the zwitterionic detergent, CHAPS, and shown that the solubilized sites bind Ins(1,4,5)P3 with an affinity (Kd = 7.26 +/- 0.52 nM, Hill coefficient h = 1.05 +/- 0.06) similar to that of the sites in native membranes (Kd = 6.02 +/- 1.57 nM, h = 0.99 +/- 0.02). ATP and a range of inositol phosphates (Ins(2,4,5)P3 Ins(4,5)P2, and inositol 1,4,5-trisphosphorothioate) also bound with similar affinities to the native and solubilized sites. Solubilization of the liver InsP3 receptor will allow its further characterization, purification, and comparison of its properties with those of InsP3 receptors already purified from cerebellum and smooth muscle.
journal_name
Cell Signaljournal_title
Cellular signallingauthors
Bond JM,Taylor CWdoi
10.1016/0898-6568(91)90037-usubject
Has Abstractpub_date
1991-01-01 00:00:00pages
607-12issue
6eissn
0898-6568issn
1873-3913pii
0898-6568(91)90037-Ujournal_volume
3pub_type
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