Effect of deglycosylation on the subunit interactions and receptor binding activity of human chorionic gonadotropin.
Effect of deglycosylation on the subunit interactions and receptor binding activity of human chorionic gonadotropin.
复制标题
去糖基化对人绒毛膜促性腺激素亚基相互作用和受体结合活性的影响。
DOI:
10.1016/s0006-291x(81)80145-3
复制
发表时间:
1981
影响因子:
3.1
通讯作者:
O. P. Bahl
中科院分区:
文献类型:
--
作者:
N. Kalyan;O. P. Bahl
The role of carbohydrate in the subunit interactions and in the binding to the receptor was assessed by the deglycosylation of the individual α- and β-subunits of hCG with trifluoromethane sulfonic acid (TFMS) at 0° for 5 h. The treatment with TFMS removed about 90% and 81% of the carbohydrates from hCG-α and hCG-β subunits respectively, without affecting the protein core as evidenced by their amino acid analyses, immunological activities and molecular weights, determined by SDS-gel electrophoresis. The deglycosylated subunits not only were able to reassociate completely as shown by the amino acid composition of the reconstituted deglycosylated hCG, but also recovered their immunological and receptor binding properties (90–105%) comparable to the native hCG. The above data strongly suggest that the carbohydrates in both subunits are not required in the interaction of the subunits and in the receptor binding activity of the hormone.