Cordero O J, Sarandeses C, Nogueira M
Department of Biochemistry and Molecular Biology, Faculty of Biology, University of Santiago de Compostela, Galicia, Spain.
FEBS Lett. 1994 Mar 14;341(1):23-7. doi: 10.1016/0014-5793(94)80233-5.
125I-Labeled prothymosin alpha (ProT alpha) was used to study the presence and characteristics of receptors for ProT alpha on human peripheral blood mononuclear cells (PBMC). The kinetics of 125I-ProT alpha binding to PBMC was fast at 37 degrees C, whilst it required 50 min to reach equilibrium at 4 degrees C and room temperature. Analysis of steady state binding data by the method of Scatchard and by unlabeled ProT alpha competition experiments identified two binding sites with an apparent equilibrium dissociation constant of 216-321 pM for the high-affinity receptor and of 11.4-21.1 nM for the low-affinity one; the sites per cell ranged from 1,479 to 1,519 and from 47,547 to 56,169, respectively. The kinetically derived equilibrium dissociation constant agreed with these data and showed no interaction between receptors.
用¹²⁵I标记的前胸腺素α（ProTα）研究ProTα在人外周血单个核细胞（PBMC）上受体的存在情况及特性。¹²⁵I-ProTα与PBMC的结合动力学在37℃时很快，而在4℃和室温下达到平衡需要50分钟。通过Scatchard方法和未标记的ProTα竞争实验对稳态结合数据进行分析，确定了两个结合位点，高亲和力受体的表观平衡解离常数为216 - 321 pM，低亲和力受体的为11.4 - 21.1 nM；每个细胞的位点数量分别为1479至1519个和47547至56169个。动力学推导的平衡解离常数与这些数据一致，且表明受体之间没有相互作用。
