| Literature DB >> 2841169 |
C A Hansen1, S vom Dahl, B Huddell, J R Williamson.
Abstract
Liver homogenates phosphorylated Ins 1,3,4-P3 to an InsP4 isomer that was distinct from Ins 1,3,4,5-P4. This InsP4 isomer accumulated in vasopressin stimulated hepatocytes prelabeled with myo-[3H]inositol with a time course that lagged behind Ins 1,3,4-P3 formation. The Ins 1,3,4-P3 kinase responsible for its formation was partially purified from rat liver. The enzyme had a Km for Ins 1,3,4-P3 of 0.29 microM, a Km for ATP of 141 microM and was not affected by changes in free Ca2+ in the physiological range. The relationship of this new InsP4 isomer to the inositol phosphate signaling pathway is discussed.Entities:
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Year: 1988 PMID: 2841169 DOI: 10.1016/0014-5793(88)80284-9
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124