D-myo-inositol 1,4,5-trisphosphate binding domain of phospholipase C-δ1

Masato Hirata, Takashi Kanematsu, Kaori Sakuma, Toshitaka Koga, Yutaka Watanabe, Shoichiro Ozaki, Hitoshi Yagisawa

Research output: Contribution to journalArticle

28 Citations (Scopus)

Abstract

D-myo-Inositol 1,4,5-trisphosphate (Ins(1,4,5)P3) binding domain of phospholipase C-δ1 (PLC-δ1) was determined by examining binding activity of the synthetic peptide corresponding to residues 30-43 of PLC-δ1. The peptide coupled with carrier proteins such as keyhole limpet hemocyanin or bovine serum albumin bound Ins(1,4,5)P3, whereas a scrambled peptide with the same amino acids did not do so. Polyclonal antibody against the peptide was examined to determine whether it would cause inhibition of the Ins(1,4,5)P3 binding to PLC-δ1. Fab fragment of antibody to the peptide did inhibit binding to PLC-δ1, in a dose-dependent manner. Thus it seems likely that the region of residues 30-43 of PLC-δ1 is responsible for the binding of Ins(1,4,5)P3.

Original languageEnglish
Pages (from-to)1563-1571
Number of pages9
JournalBiochemical and Biophysical Research Communications
Volume205
Issue number3
DOIs
Publication statusPublished - 1994

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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