The role of the carbohydrate moiety in thyrotropin action

The relative binding affinity of deglycosylated human TSH was 6-fold higher than that of native TSH. Although deglycosylated human TSH significantly stimulated adenlyate cyclase, it was less effective than the native hormone. When deglycosylated human TSH was added with bovine TSH, however, a dose-dependent antagonism was observed. In particular, submaximal and maximal concentrations of bovine TSH and deglycosylated human TSH resulted in cAMP values much lower than the sum of activities of the individual hormones. The data suggest that although the effects of TSH deglycosylation are not as dramatic as with the gonadotropins, the carbohydrates of TSH appear to be required for maximal activation of adenylate cyclase by the hormone.