Ferrara P, Li C H
Proc Natl Acad Sci U S A. 1980 Oct;77(10):5746-8. doi: 10.1073/pnas.77.10.5746.
The interaction of human beta-endorphin with binding sites in rabbit spinal cord has been characterized. The stereospecific high-affinity binding sites are concentrated in the dorsal half of the spinal cord. Scatchard analysis of the binding data shows heterogeneity of the binding sites that can be resolved into two populations with apparent dissociation constants of 3.0 (+/-2.0) X 10(-10) and 3.3 (+/- 0.5) X 10(-9) M. Sodium ions decrease the binding of human beta-endorphin to spinal cord to the same extent as found in rat brain. The ability of several opiates and opioid peptides to inhibit the binding of human beta-endorphin is also presented.
已对人β-内啡肽与兔脊髓中结合位点的相互作用进行了表征。立体特异性高亲和力结合位点集中在脊髓的背侧半部。对结合数据的Scatchard分析表明,结合位点具有异质性,可分为两个群体,其表观解离常数分别为3.0(±2.0)×10⁻¹⁰和3.3(±0.5)×10⁻⁹ M。钠离子降低人β-内啡肽与脊髓的结合程度与在大鼠脑中发现的程度相同。还介绍了几种阿片类药物和阿片样肽抑制人β-内啡肽结合的能力。