Pliam N B, Nyiredy K O, Arnaud C D
Proc Natl Acad Sci U S A. 1982 Mar;79(6):2061-3. doi: 10.1073/pnas.79.6.2061.
We have demonstrated binding of synthetic bovine parathyroid hormone (1-34) [bPTH-(1-34)] to embryonic avian bone cells in monolayer culture. The binding sites have qualitative and quantitative characteristics of a physiologically important parathyroid hormone (PTH) receptor. At apparent steady state (60 min at 24 degrees C), 5-10% of electrolytically labeled, receptor-purified 125I-labeled bPTH-(1-34) bound specifically to the cells whereas nonspecific binding was less than 1% of the added labeled hormone. Scatchard analysis showed a single order of PTH binding sites (Kd = 0.6 nM) with approximately 10,000 sites per cell. In this bone cell system, PTH bound to its binding site and stimulated cAMP accumulation over the same concentration range. Bovine PTH-(1-84) bound to the cells with the same apparent affinity as bPTH-(1-34).
我们已经证明，合成的牛甲状旁腺激素（1-34）[bPTH-(1-34)]能与单层培养的胚胎禽骨细胞结合。这些结合位点具有生理上重要的甲状旁腺激素（PTH）受体的定性和定量特征。在明显的稳态（24℃下60分钟）时，5%-10%经电解标记、受体纯化的125I标记的bPTH-(1-34)特异性结合到细胞上，而非特异性结合小于添加的标记激素的1%。Scatchard分析显示有单一顺序的PTH结合位点（Kd = 0.6 nM），每个细胞约有10,000个位点。在这个骨细胞系统中，PTH与其结合位点结合，并在相同浓度范围内刺激cAMP积累。牛PTH-(1-84)与细胞结合的表观亲和力与bPTH-(1-34)相同。
