Woods D J, Monaco M E
Department of Physiology and Biophysics, New York University Medical Center, New York 10016.
Mol Endocrinol. 1988 Apr;2(4):350-4. doi: 10.1210/mend-2-4-350.
Specific vasopressin binding to WRK-1 rat mammary tumor cells was assessed and compared with vasopressin-induced alterations in phosphatidylinositol metabolism. Scatchard analysis revealed the presence of two binding sites: a saturable, high affinity site with a dissociation constant of 1 X 10(-9) M and an n of 2700 sites per cell, and a nonsaturable, apparent lower affinity site. The higher affinity site appeared to have V1a specificity and to correlate with vasopressin's ability to stimulate phosphatidylinositol turnover in the cells.
评估了特异性血管加压素与WRK-1大鼠乳腺肿瘤细胞的结合情况，并将其与血管加压素诱导的磷脂酰肌醇代谢变化进行了比较。Scatchard分析显示存在两个结合位点：一个可饱和的高亲和力位点，解离常数为1×10(-9) M，每个细胞有2700个位点，以及一个不饱和的、表观亲和力较低的位点。较高亲和力的位点似乎具有V1a特异性，并与血管加压素刺激细胞中磷脂酰肌醇周转的能力相关。
