Köppler P, Mersel M, Humbert J P, Vignon J, Vincendon G, Malviya A N
Laboratoire de Neurobiologie Moléculaire des Interactions Cellulaires, Centre National de la Recherche Scientifique, Strasbourg, France.
Biochemistry. 1996 Apr 30;35(17):5481-7. doi: 10.1021/bi9522918.
Inositol 1,3,4,5-tetrakisphosphate (InsP4) mediates nuclear calcium signalling [Köppler P., Matter, N., Malviya A.N. (1993) J. Biol. Chem. 268, 26248-26252], and a distinct high affinity InsP4 binding site is identified with rat liver nuclei [Köppler, P., Mersel, M., & Malviya, A.N. (1994) Biochemistry 33, 14707-14713] as compared with other rat liver membrane fractions. A novel InsP4 receptor protein derived from rat liver nuclei has been purified to apparent homogeneity employing preparative isoelectric focusing, electrophoretic mobility, nondenaturating polyacrylamide gel electrophoresis, and electroelution. Isoelectric focusing indicated an isoelectric pH around 4.3 +/- 0.2 which was further confirmed by bidimensional electrophoresis. The high affinity nuclear InsP4 receptor was identified as a 74 kDa protein both on the SDS-PAGE and on the bidimensional electrophoresis. Partial microsequence analysis showed that the N-terminal end of nuclear InsP4 receptor consists of amino acids: PNHKNEIAGNFS. The 74 kDa nuclear InsP4 receptor protein is a distinct protein from the other InsP4 receptors purified from other sources and documented in the literature.
肌醇1,3,4,5 - 四磷酸（InsP4）介导细胞核钙信号传导[Köppler P., Matter, N., Malviya A.N.（1993）《生物化学杂志》268, 26248 - 26252]，并且与大鼠肝脏的其他膜组分相比，在大鼠肝细胞核中鉴定出了一个独特的高亲和力InsP4结合位点[Köppler, P., Mersel, M., & Malviya, A.N.（1994）《生物化学》33, 14707 - 14713]。利用制备性等电聚焦、电泳迁移率、非变性聚丙烯酰胺凝胶电泳和电洗脱技术，从大鼠肝细胞核中纯化出一种新型的InsP4受体蛋白，达到了明显的均一性。等电聚焦显示等电点pH约为4.3±0.2，二维电泳进一步证实了这一点。在SDS - PAGE和二维电泳上，高亲和力的细胞核InsP4受体均被鉴定为一种74 kDa的蛋白质。部分微序列分析表明，细胞核InsP4受体的N末端由氨基酸PNHKNEIAGNFS组成。74 kDa的细胞核InsP4受体蛋白与从其他来源纯化并在文献中记载的其他InsP4受体是不同的蛋白质。
