Grandics P, Puri R K, Toft D O
Endocrinology. 1982 Mar;110(3):1055-7. doi: 10.1210/endo-110-3-1055.
A new steroid affinity resin has been developed which can be successfully used to partially purify the non-transformed species of the progesterone receptor from chick oviduct. Deoxycorticosterone has been modified through its 21-carbon and linked to a stable spacer arm which is attached to Sepharose 2B by an epoxide technique. The affinity resin is very resistant to chemical breakdown or to enzymatic destruction in crude tissue extracts. We have standardized the capacity and optimum conditions for elution of receptor which is bound to the affinity resin. Receptor purification of several hundred-fold can be obtained routinely with good yield. The cytosol receptor prepared in the presence of sodium molybdate remains in the non-transformed 8S state following affinity chromatography.
一种新型甾体亲和树脂已被研制出来，它可成功用于从鸡输卵管中部分纯化孕酮受体的非转化形式。脱氧皮质酮已通过其21-碳位进行修饰，并与一个稳定的间隔臂相连，该间隔臂通过环氧技术连接到琼脂糖2B上。这种亲和树脂在粗组织提取物中对化学分解或酶解具有很强的抵抗力。我们已经确定了与亲和树脂结合的受体的洗脱容量和最佳条件。常规情况下，受体可获得数百倍的纯化，且产率良好。在钼酸钠存在下制备的胞质溶胶受体在亲和层析后仍保持非转化的8S状态。
