Turyn D, Santomé J A, Dellacha J M, Stringa de Muzzio I G, Domergasso C S
Acta Physiol Lat Am. 1976;26(5):395-402.
Specific binding of 125I-HGH and 125I-bGH was obtained in hypophysectomized rat liver cells. Two types of somatogenic receptors were found with apparent dissociation constants of 4.2 x 10(8) M-1 and 1.7 x 10(7) M-1. The number of sites for the higher and lower affinity receptors were: 1 x 10(4) and 6 x 10(3), respectively. Human, bovine and equine growth hormones appear to bind to liver cells with equal affinity, while ovine prolactin needs at least a two-order-magnitude greater concentration to displace 125I-bGH. A parallelism between biological activity and binding data was observed.
在垂体切除的大鼠肝细胞中获得了¹²⁵I-人生长激素(¹²⁵I-HGH)和¹²⁵I-牛生长激素(¹²⁵I-bGH)的特异性结合。发现了两种促生长受体,其表观解离常数分别为4.2×10⁻⁸ M⁻¹和1.7×10⁻⁷ M⁻¹。高亲和力和低亲和力受体的位点数量分别为:1×10⁴和6×10³。人、牛和马生长激素似乎以相等的亲和力与肝细胞结合,而绵羊催乳素需要至少高两个数量级的浓度才能取代¹²⁵I-bGH。观察到生物活性与结合数据之间存在平行关系。