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Distinct binding sites for inositol 1 4 5 triphosphate and inositol 1 3 4 5 tetrakisphosphate in bovine parathyroid glands



Distinct binding sites for inositol 1 4 5 triphosphate and inositol 1 3 4 5 tetrakisphosphate in bovine parathyroid glands



Biochemical & Biophysical Research Communications 159(1): 200-208



We utilized high specific activity, [32P]-labelled ligands to measure the binding of Ins(1,3,4,5)P4 and Ins(1,4,5)P3 to membranes prepared from bovine parathyroid glands. [32P]Ins(1,3,4,5)P4 bound rapidly and reversibly to parathyroid membranes, and the binding data could be fitted by the interaction of the ligand with two sites, one with Kd = 6.8 .times. 10-9 M and Bmax = 26 fmol/mg protein and a second, lower affinity site, with Kd = 4.1 .times. 10-7 M and Bmax = 400 fmol/mg protein. InsP5 was 10-20 fold less potent than InsP4, and Ins(1,3,4)P3 and Ins(1,4,5)P3 were nearly 1000-fold less potent in displacing [32P]Ins(1,3,4,5)P4. [32P]Ins(1,4,5)P3, on the other hand, bound to a single class of sites with Kd = 7.6 .times. 10-9 M and Bmax = 34 fmol/mg. While the binding of [32P]Ins(1,4,5)P3 increased markedly on raising pH from 5 to 8, the binding of [32P]Ins(1,3,4,5)P4 decreased by 75% over this range of pH. Thus, [32P]-labelled Ins(1,3,4,5)P4 and Ins(1,4,5)P3 may be used to identify distinct binding sites which may represent physiologically relevant intracellular receptors for InsP3 and InsP4 in parathyroid cells.

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