Ca2+/calmodulin independent inositol 1,4,5-trisphosphate 3-kinase activity in guinea pig peritoneal macrophages

Yuichi Kimura, Yutaka Watanabe, Shoichiro Ozaki, Toshitaka Koga, Masato Hirata

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)

Abstract

1. 1. The Ca2+/calmodulin (CaM) independent activity of inositol 1,4,5-trisphosphate (InsP3) 3-kinase in macrophages could be separated from the dependent activity by serial column chromatography, gel filtration, Orange A and DEAE-5PW. 2. 2. An InsP3 analog which has an aminobenzoyl group on the 2nd carbon of the inositol ring inhibited the conversion of [3H]InsP3 to [3H]InsP4 (inositol 1,3,4,5-tetrakisphosphate) in a dose-dependent manner. The concentration required for half-maximal inhibition (IC50) with the Ca2+/CaM independent enzyme activity was also dependent on the free Ca2+ concentration, as with the dependent activity. 3. 3. These results suggest that a conformational change in the enzyme occurs in response to a change in free Ca2+ concentration, and thus the potency to recognize the InsP3 analog would change, even when the Ca2+ CaM independent enzyme activity was used.

Original languageEnglish
Pages (from-to)527-533
Number of pages7
JournalComparative Biochemistry and Physiology -- Part B: Biochemistry and
Volume97
Issue number3
DOIs
Publication statusPublished - 1990

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Physiology
  • Molecular Biology

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