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.
|Number of pages||7|
|Journal||Comparative Biochemistry and Physiology -- Part B: Biochemistry and|
|Publication status||Published - 1990|
All Science Journal Classification (ASJC) codes
- Molecular Biology