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

J M Bond, C W Taylor

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)607-12
Number of pages6
JournalCellular signalling
Issue number6
Publication statusPublished - 1991


  • Animals
  • Binding Sites
  • Calcium
  • Calcium Channels
  • Hydrogen-Ion Concentration
  • Inositol 1,4,5-Trisphosphate
  • Inositol 1,4,5-Trisphosphate Receptors
  • Liver
  • Male
  • Rats
  • Rats, Inbred Strains
  • Receptors, Cell Surface
  • Receptors, Cytoplasmic and Nuclear
  • Solubility


Dive into the research topics of 'Solubilization of rat liver inositol 1,4,5-trisphosphate receptor'. Together they form a unique fingerprint.

Cite this