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

研究成果: Contribution to journalArticle査読

28 被引用数 (Scopus)

抄録

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.

本文言語英語
ページ(範囲)1563-1571
ページ数9
ジャーナルBiochemical and Biophysical Research Communications
205
3
DOI
出版ステータス出版済み - 1994

All Science Journal Classification (ASJC) codes

  • 生物理学
  • 生化学
  • 分子生物学
  • 細胞生物学

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