Phillips Burnett C C, Anderson W A, Rüchel R
J Histochem Cytochem. 1978 May;26(5):382-90. doi: 10.1177/26.5.659839.
Estrogen-dependent peroxidase from rat uterine fluid has been investigated by microelectrophoretic techniques. The molecular weight of the enzyme has been determined in the range of 100,000 by using polyacrylamide gradient gels in the absence and presence of nonionic and anionic detergent. The isoelectric points are located between pH 4.5 and 5.9. Employing the two-dimensional combination of isoelectric focusing and gel gradient electrophoresis, the enzyme was separated into two subunits, one having a molecular weight of 70,000, the other less than 20,000. The large subunit has slight enzymatic activiy, while the smaller subunit may be responsible for the charge difference in the holoenzyme pattern. The glycoprotein pattern of the uterine fluid peroxidase is further defined by its separation by affinity chromatography using a concanavalin A-Sepharose column and by its susceptibility to neuraminidase treatment.
已采用微电泳技术对大鼠子宫液中的雌激素依赖性过氧化物酶进行了研究。在不存在和存在非离子及阴离子去污剂的情况下，使用聚丙烯酰胺梯度凝胶测定了该酶的分子量在100,000范围内。其等电点位于pH 4.5至5.9之间。利用等电聚焦和凝胶梯度电泳的二维组合，该酶被分离为两个亚基，一个亚基的分子量为70,000，另一个小于20,000。大亚基具有轻微的酶活性，而较小的亚基可能导致全酶图谱中的电荷差异。子宫液过氧化物酶的糖蛋白图谱通过使用伴刀豆球蛋白A - 琼脂糖柱进行亲和层析分离以及对其进行神经氨酸酶处理的敏感性进一步确定。
