López de Haro M S, Pérez Martínez M, Nieto A
Centro de Biología Molecular (CSIC-UAM), Universidad Autónoma, Cantoblanco, Madrid, Spain.
Biochem Int. 1992 Jul;27(2):251-6.
Rabbit uteroglobin was purified from both uterine fluids and lung lavages by a combination of gel filtration and ion-exchange column chromatography. Anti-trypsin and anti-papain activities were measured in the fractions of the eluates. Anti-proteinase activities were detected in minor contaminants eluting close to the uteroglobin peak but the protein itself was devoid of anti-proteinase activity. Ion-exchange-purified uteroglobin also lacked inhibitory activity of elastase, chymotrypsin or subtilisin. The presence of contaminants could explain the anti-proteinase activity reported occasionally for uteroglobin.
通过凝胶过滤和离子交换柱色谱相结合的方法，从兔子宫液和肺灌洗液中纯化出兔子宫珠蛋白。对洗脱液各组分进行抗胰蛋白酶和抗木瓜蛋白酶活性检测。在靠近子宫珠蛋白峰洗脱的少量污染物中检测到抗蛋白酶活性，但该蛋白本身缺乏抗蛋白酶活性。经离子交换纯化的子宫珠蛋白也缺乏对弹性蛋白酶、胰凝乳蛋白酶或枯草杆菌蛋白酶的抑制活性。污染物的存在可以解释偶尔报道的子宫珠蛋白的抗蛋白酶活性。
