Solubilization of rat liver inositol 1,4,5-trisphosphate receptor.

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 Signal

journal_title

Cellular signalling

authors

Bond JM,Taylor CW

doi

10.1016/0898-6568(91)90037-u

subject

Has Abstract

pub_date

1991-01-01 00:00:00

pages

607-12

issue

6

eissn

0898-6568

issn

1873-3913

pii

0898-6568(91)90037-U

journal_volume

3

pub_type

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