Solubilization and separation of inositol 1,3,4,5-tetrakisphosphate- and inositol 1,4,5-trisphosphate-binding proteins and metabolizing enzymes in rat brain

A. B. Theibert, S. Supattapone, C. D. Ferris, S. K. Danoff, R. K. Evans, S. H. Snyder

Research output: Contribution to journalArticlepeer-review

29 Scopus citations

Abstract

The two inositol phosphate-binding proteins, the Ins(1,4,5)P3 (InsP3) and Ins(1,3,4,5)P4 (InsP4) receptors, and the two particulate InsP3-metabolizing enzymes, InsP3 5-phosphatase and InsP3 3-kinase, were solubilized with detergent from rat cerebellar membranes. These four activities are shown to be distinct molecular species by separation using a variety of protein chromatographic steps. The pharmacology of the partially purified InsP4-binding site indicates that the binding has a high affinity and selectivity for InsP4 over InsP3. These results suggest the existence of a distinct specific InsP4-binding protein which may represent the receptor for this putative second messenger.

Original languageEnglish (US)
Pages (from-to)441-445
Number of pages5
JournalBiochemical Journal
Volume267
Issue number2
DOIs
StatePublished - 1990

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint

Dive into the research topics of 'Solubilization and separation of inositol 1,3,4,5-tetrakisphosphate- and inositol 1,4,5-trisphosphate-binding proteins and metabolizing enzymes in rat brain'. Together they form a unique fingerprint.

Cite this