Bradford P G, Irvine R F
Department of Pharmacology, Hahnemann University, Philadelphia, PA 19102-1192.
Biochem Biophys Res Commun. 1987 Dec 16;149(2):680-5. doi: 10.1016/0006-291x(87)90421-9.
Membranes of HL-60 cells were shown to possess saturable binding sites for [3H]inositol(1,3,4,5)tetrakisphosphate, with nanomolar affinity (KD = 90 nM) and a density of 250 fmol/mg protein. The specificity of the binding sites for Ins(1,3,4,5)P4 was assessed by competition studies utilising a variety of inositol polyphosphates; results indicated that both the presence and the correct grouping of the phosphates were important for high affinity recognition. The apparent affinity of the binding sites for Ins(1,3,4,5)P4 was over 200-fold greater than for Ins(1,4,5)P3. The possibility is discussed that this binding site represents the receptor which mediates the action of Ins(1,3,4,5)P4 as a putative intracellular second messenger.
HL-60细胞的膜被证明具有对[3H]肌醇(1,3,4,5)四磷酸的可饱和结合位点,具有纳摩尔亲和力(KD = 90 nM),密度为250 fmol/mg蛋白质。通过使用多种肌醇多磷酸的竞争研究评估了Ins(1,3,4,5)P4结合位点的特异性;结果表明,磷酸基团的存在和正确分组对于高亲和力识别都很重要。Ins(1,3,4,5)P4结合位点的表观亲和力比对Ins(1,4,5)P3的亲和力高200多倍。文中讨论了这种结合位点可能代表介导Ins(1,3,4,5)P4作为假定细胞内第二信使作用的受体。