Abstract
Turkey erythrocytes contain soluble and particulate kinase activities which catalyse the ATP-dependent phosphorylation of inositol 1,4,5-trisphosphate [Ins(1,4,5)P3]. The particle-bound activity accounts for approximately one-quarter of the total cellular Ins(1,4,5)P3 kinase, when assayed at a [Ca2+] of 10 nM. The particle-bound Ins(1,4,5)P3 kinase is not washed from the membrane by 0.6 M-KCl, yet may be solubilized by a variety of detergents. This suggests that it is an intrinsic membrane protein. The product of the membrane-bound Ins(1,4,5)P3 kinase is inositol 1,3,4,5-tetrakisphosphate [Ins(1,3,4,5)P4], identifying the enzyme as an Ins(1,4,5)P3 3-kinase. In the presence of calmodulin, the membrane-associated Ins(1,4,5)P3 3-kinase is activated as [Ca2+] is increased over the range 0.2-1.0 microM. Under these conditions, the rates of dephosphorylation of Ins(1,3,4,5)P4 and Ins(1,4,5)P3 by phosphatases in the membrane fraction are unchanged.
Dates
Type | When |
---|---|
Created | 10 years ago (Aug. 10, 2015, 5:09 p.m.) |
Deposited | 3 years, 9 months ago (Nov. 25, 2021, 12:57 p.m.) |
Indexed | 1 year, 7 months ago (Jan. 12, 2024, 5:39 a.m.) |
Issued | 37 years, 9 months ago (Dec. 1, 1987) |
Published | 37 years, 9 months ago (Dec. 1, 1987) |
Published Print | 37 years, 9 months ago (Dec. 1, 1987) |
@article{Morris_1987, title={Turkey erythrocytes possess a membrane-associated inositol 1,4,5-trisphosphate 3-kinase that is activated by Ca2+ in the presence of calmodulin}, volume={248}, ISSN={1470-8728}, url={http://dx.doi.org/10.1042/bj2480489}, DOI={10.1042/bj2480489}, number={2}, journal={Biochemical Journal}, publisher={Portland Press Ltd.}, author={Morris, A J and Downes, C P and Harden, T K and Michell, R H}, year={1987}, month=dec, pages={489–493} }