Delvaux A, Dumont J E, Erneux C
Biochem Biophys Res Commun. 1987 May 29;145(1):59-65. doi: 10.1016/0006-291x(87)91287-3.
Rat brain soluble fraction contains an enzymatic activity that dephosphorylates inositol 1,4-bisphosphate (Ins(1,4)P2). We have used anion exchange h.p.l.c. in order to identify the inositol monophosphate product of Ins(1,4)P2 hydrolysis (i.e. Ins(1)P1, Ins(4)P1 or both). When [3H]Ins(1,4)P2 was used as substrate, we obtained an inositol monophosphate isomer that was separated from the co-injected standard [3H]Ins(1)P1. This suggested an Ins(1,4)P21-phosphatase pathway leading to the production of the inositol 4-monophosphate isomer. The dephosphorylation of [32P]Ins(4)P1 was measured in rat brain, liver and heart soluble fraction and was Li+-sensitive. Chromatography of the soluble fraction of a rat brain homogenate on DEAE-cellulose resolved a monophosphate phosphatase activity that hydrolyzed both [3H]Ins(1)P1 and [4-32P]Ins(4)P1 isomers.
大鼠脑可溶性组分含有一种可使肌醇-1,4-二磷酸(Ins(1,4)P2)去磷酸化的酶活性。我们使用阴离子交换高效液相色谱法来鉴定Ins(1,4)P2水解产生的肌醇单磷酸产物(即Ins(1)P1、Ins(4)P1或两者)。当使用[3H]Ins(1,4)P2作为底物时,我们获得了一种肌醇单磷酸异构体,它与共注入的标准[3H]Ins(1)P1分离。这表明存在一条Ins(1,4)P2 1-磷酸酶途径,可导致产生肌醇4-单磷酸异构体。在大鼠脑、肝和心脏可溶性组分中测定了[32P]Ins(4)P1的去磷酸化,并且其对Li+敏感。大鼠脑匀浆的可溶性组分在DEAE-纤维素上进行色谱分离,得到一种单磷酸磷酸酶活性,它可水解[3H]Ins(1)P1和[4-32P]Ins(4)P1两种异构体。