D-myo-inositol 1,4,5-trisphosphate-binding proteins in rat brain membranes

Masako Yoshida, Takashi Kanematsu, Yutaka Watanabe, Toshitaka Koga, Shoichiro Ozaki, Sadaaki Iwanaga, Masato Hirata

研究成果: ジャーナルへの寄稿学術誌査読

61 被引用数 (Scopus)


Rat brain membrane fractions obtained using Triton X-100 were applied to a D-myo-inositol 1,4,5-trisphosphate [D-Ins(1,4,5)P3] immobilized column, followed by gel filtration and anion-exchange chromatography. Two proteins with molecular masses of 130 and 85 kDa, as assessed by SDS-polyacrylamide gel electrophoresis, were purified to apparent homogeneity as D-[3H] Ins(1,4,5)P3-binding proteins with no D-Ins(1,4,5)P3-metabolizing activity. Partial amino acid sequence determinations of these proteins revealed that the 130 kDa protein appears to be a new D-Ins(1,4,5)P3-binding protein and the 85 kDa protein is δ1-isozyme of phospholipase C. We have previously purified 130 and 85 kDa proteins, as D-[3H]Ins(1, 4, 5)P3-binding proteins, from rat brain cytosol fraction. Antibodies against the 130 kDa protein from the cytosol cross-reacted with the membrane 130 kDa protein purified in this study, suggesting that the membrane 130 kDa protein is likely to be the same as the protein from the cytosol fraction. The inhibition of D-[3H]Ins(1,4,5)P3 binding by D-isomers of inositol phosphates available clarified that the 130 kDa protein has a similar affinity for D-Ins(1,4,5,6)P4 to that for D-Ins(1,4,5)P3, while the 85 kDa protein is specific to D-Ins(1,4,5)P3.

ジャーナルJournal of biochemistry
出版ステータス出版済み - 5月 1994

!!!All Science Journal Classification (ASJC) codes

  • 生化学
  • 分子生物学


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