Ghiani B U, Masini M A
Istituto di Anatomia Comparata, Università di Genova, Italy.
Comp Biochem Physiol A Physiol. 1995 Jul;111(3):439-44. doi: 10.1016/0300-9629(95)00030-b.
Specific 125I angiotensin II binding sites were identified in the rat pancreas by radioreceptor assay, autoradiography and immunohistochemistry. Scatchard analysis of the binding in normal rats yielded a Kd of 0.51 +/- 0.23 nM with a Bmax of 15 +/- 3.5 fmol/mg protein (means +/- SD, n = 6). Changed plasma sodium concentration resulted in modifications in the binding affinity and capacity. Sodium loading depressed both Kd (0.36 +/- 0.1 nM) and Bmax (6.4 +/- 0.1 fmol/mg protein), while sodium depletion elevated both Kd (2.03 +/- 0.3 nM) and Bmax (45 +/- 3.5 fmol/mg protein) (means +/- SD, n = 6). Autoradiography using 125I Ang II and immunohistochemistry of the binding sites saturated with unlabeled Ang II and incubated with Ab-Ile5 Ang II, revealed localization of the binding sites on the islet cell membranes and in the exocrine pancreas.
通过放射受体分析、放射自显影和免疫组织化学在大鼠胰腺中鉴定出特异性的125I血管紧张素II结合位点。对正常大鼠结合情况的Scatchard分析得出解离常数(Kd)为0.51±0.23 nM,最大结合容量(Bmax)为15±3.5 fmol/mg蛋白质(平均值±标准差,n = 6)。血浆钠浓度的改变导致结合亲和力和结合容量发生变化。钠负荷降低了Kd(0.36±0.1 nM)和Bmax(6.4±0.1 fmol/mg蛋白质),而钠缺乏则提高了Kd(2.03±0.3 nM)和Bmax(45±3.5 fmol/mg蛋白质)(平均值±标准差,n = 6)。使用125I血管紧张素II的放射自显影以及用未标记的血管紧张素II饱和并与Ab-Ile5血管紧张素II孵育后的结合位点免疫组织化学显示,结合位点定位于胰岛细胞膜和外分泌胰腺中。