Dilley W G, Haagensen D E, Cox C E, Wells S A
Department of Surgery, Washington University School of Medicine, St. Louis, Missouri 63110.
Breast Cancer Res Treat. 1990 Oct;16(3):253-60. doi: 10.1007/BF01806333.
A major protein of human breast cyst fluid, termed GCDFP-24, has the property of specifically binding progestins. The purified glycoprotein, of 24,000 apparent molecular weight, bound pregnenolone and progesterone with highest affinity. The association constant for binding of progesterone was 1 X 10(6)L/mol by Scatchard analysis, and there was one binding site per molecule. Changes to the progesterone structure at C-17, C-20, or C-21 interfered with binding. The pH optimum for binding was 4-4.5. The purified protein was highly stable and was not irreversibly denatured by 50% methanol or 3M guanidine. However, dithiothreitol reversibly interfered with progesterone binding. Rabbit antiserum produced against the glycoprotein recognized an immunologically identical component in normal human sera, and partially cross-reacting components in normal monkey and baboon sera. The component in human sera was present in Cohn fractions IV and VI.
人乳腺囊肿液中的一种主要蛋白质，称为GCDFP - 24，具有特异性结合孕激素的特性。纯化后的糖蛋白表观分子量为24,000，与孕烯醇酮和孕酮的结合亲和力最高。通过Scatchard分析，孕酮结合的缔合常数为1×10⁶L/mol，每个分子有一个结合位点。C - 17、C - 20或C - 21位孕酮结构的改变会干扰结合。结合的最适pH为4 - 4.5。纯化后的蛋白质高度稳定，不会被50%甲醇或3M胍不可逆地变性。然而，二硫苏糖醇会可逆地干扰孕酮结合。针对该糖蛋白产生的兔抗血清识别正常人血清中免疫相同的成分，以及正常猴和狒狒血清中部分交叉反应的成分。人血清中的该成分存在于Cohn组分IV和VI中。
