TAMM-HORSFALL URINARY GLYCOPROTEIN - SUBUNIT STRUCTURE
TAMM-HORSFALL URINARY GLYCOPROTEIN - SUBUNIT STRUCTURE
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DOI：
10.1042/bj1200425
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发表时间：
1970-01-01
影响因子：
4.1
通讯作者：
RATCLIFFE, WA
中科院分区：
文献类型：
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作者：
FLETCHER, AP;NEUBERGER, A;RATCLIFFE, WA
1.在十二烷基硫酸钠存在下，Sephadex G-200凝胶过滤得到天然的和烷基化的Tamm-Horsfall糖蛋白的亚基相对分子质量为76000-82000。2.经十二烷基硫酸钠圆盘凝胶电泳法测得亚基相对分子质量为79000±4000.3.溴化氰裂解糖蛋白所释放的N-末端氨基酸的最小化学相对分子质量为79000±6000.4.囊性纤维化患者Tamm-Horsfall糖蛋白的亚基相对分子质量与正常对照组相近。5.在1.0%十二烷基硫酸钠和70%甲酸中超速离心时，Tamm-Horsfall糖蛋白以单一组分的形式沉淀，略快于血清白蛋白。6.在还原二硫键时，得到了相同的亚单位分子量，这表明这些键是链内的。
1. Subunit molecular weights of 76000–82000 were obtained for native and alkylated Tamm–Horsfall glycoprotein by gel filtration on Sephadex G-200 in the presence of sodium dodecyl sulphate. 2. A further estimate of the subunit molecular weight of 79000±4000 was obtained by disc gel electrophoresis in sodium dodecyl sulphate. 3. A minimum value of the chemical molecular weight of 79000±6000 was obtained from the number ofN-terminal amino acids released by cyanogen bromide cleavage of the glycoprotein. 4. Similar values were obtained for the subunit molecular weight of Tamm–Horsfall glycoprotein from patients with cystic fibrosis. 5. On ultracentrifugation both in 1.0% sodium dodecyl sulphate and in 70% formic acid, Tamm–Horsfall glycoprotein sedimented as a single component, slightly faster than serum albumin. 6. On reduction of the disulphide bonds the same subunit molecular weight was obtained, which suggested that these bonds are intrachain.