Lynn K L, Marshall R D
Biochem J. 1981 Feb 15;194(2):561-8. doi: 10.1042/bj1940561.
Affinity chromatography, with rabbit anti-(human Tamm-Horsfall glycoprotein) IgG, was applied to the isolation from normal human serum of protein, which is immunologically cross-reactive with the urinary glycoprotein. The antigen-antibody complex was dissociated with the use of sodium thiocyanate solution, a medium which fails to dissociate urinary Tamm-Horsfall glycoprotein-antigen complex. The cross-reactive serum proteins were isolated in amounts of 19-24 mg/l of serum. They have apparent molecular weights, assessed by disc-gel electrophoresis in the presence of sodium dodecyl sulphate, of 125 000, 84 000 and 74 000 respectively, with mobilities differing from that of urinary Tamm-Horsfall glycoprotein. They have a much lower immunoreactivity towards the antibody than does the urinary glycoprotein. Tamm-Horsfall glycoprotein could not be demonstrated in normal serum by the techniques used. The implications of these findings are discussed in terms of pathology involving Tamm-Horsfall glycoprotein.
采用兔抗（人Tamm-Horsfall糖蛋白）IgG亲和层析法，从正常人血清中分离出与尿糖蛋白有免疫交叉反应的蛋白质。抗原-抗体复合物用硫氰酸钠溶液解离，该介质不能解离尿Tamm-Horsfall糖蛋白-抗原复合物。交叉反应血清蛋白的分离量为每升血清19 - 24毫克。通过十二烷基硫酸钠存在下的圆盘凝胶电泳评估，它们的表观分子量分别为125000、84000和74000，迁移率与尿Tamm-Horsfall糖蛋白不同。它们对抗体的免疫反应性比尿糖蛋白低得多。所用技术未能在正常血清中检测到Tamm-Horsfall糖蛋白。从涉及Tamm-Horsfall糖蛋白的病理学角度讨论了这些发现的意义。
