Moyer J D, Reizes O, Dean N M, Malinowski N
Biochem Biophys Res Commun. 1987 Aug 14;146(3):1018-26. doi: 10.1016/0006-291x(87)90749-2.
A specific 1-phosphatase acting on myo-inositol (1,4)-biphosphate with a high affinity (Km = 0.9 microM) has been purified 49-fold from soluble proteins of rat liver by anion exchange chromatography followed by gel filtration. This enzyme has a molecular weight of 58,000 as estimated by gel filtration, a pH optimum of 7.5, and requires Mg++ for activity. The only product formed from myo-inositol (1,4)-bisphosphate is the 4-monophosphate. Of 7 other inositol phosphates examined only myo-inositol (1,3,4)-triphosphate was a substrate.