通过亲和光谱法评估3H-CGP 12177和3H-DHA与大鼠网织红细胞β2-肾上腺素能受体的结合。
Evaluation of 3H-CGP 12177 and 3H-DHA binding to beta 2-adrenoceptors of rat reticulocytes by means of affinity spectra.
作者信息
Kállay Z, Smisterová J, Soltés L, Marko V
机构信息
Institute of Preventive and Clinical Medicine, Bratislava, Czecho-Slovakia.
出版信息
J Recept Res. 1991;11(6):909-17. doi: 10.3109/10799899109064687.
3H-CGP 12177 and 3H-DHA binding to rat reticulocyte beta 2-adrenoceptors by using an excess of 1 x 10(-5) mol l-1 propranolol was evaluated by means of affinity spectra. To describe the 3H-CGP 12177 interaction with rat reticulocytes a binding isotherm valid for one single class of specific binding sites was found to be satisfactory. On the other hand, a more complex binding isotherm had to be used for the description of the 3H-DHA interaction with rat reticulocytes. This observation further supports the preferred application of 3H-CGP 12177 over 3H-DHA for radio-receptor assay of beta-adrenoceptor blockers.
通过亲和光谱法评估了在存在过量1×10⁻⁵ mol l⁻¹普萘洛尔的情况下，³H-CGP 12177和³H-DHA与大鼠网织红细胞β₂-肾上腺素能受体的结合。为描述³H-CGP 12177与大鼠网织红细胞的相互作用，发现适用于单一类特异性结合位点的结合等温线是令人满意的。另一方面，对于³H-DHA与大鼠网织红细胞相互作用的描述，则必须使用更复杂的结合等温线。这一观察结果进一步支持了在β-肾上腺素能受体阻滞剂的放射受体测定中，³H-CGP 12177比³H-DHA更适合应用。
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