By Jacob Robbins (auth.), Ragnar Ekholm, Leonard D. Kohn, Seymour H. Wollman (eds.)
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Extra info for Control of the Thyroid Gland: Regulation of Its Normal Function and Growth
L40-l43 After incubation of mouse thyrotrophic tumor tissue with 35S- me thionine for 10-minutes, most a-subunits were of molecular weight 18,000, while only a few were 21,000 daltons. When the pulse incubation was followed by chase incubations of variable length, the 18,000 form of a-subunit was THYROID STIMULATING HORMONE: STRUCTURE AND FUNCTION 41 progressive1y converted to the 21,000 form. After treatment with endog1ycosidase H, both the 18,000 and 21,000 mo1ecu1ar weight forms of a-subunit were converted to an 11,000 form 141 ,143, consistent with the weight of the apoprotein portion of standard a-subunit.
159 Man a GlcNAc 2 oligosaccharides became particularly prominent on a-subunits of heterodimers after chase incubations, or after prolonged pulse incubations, and this phenomenon was observed in pituitaries from euthyroid and hypothyroid mice as well as in mouse thyrotrophic tumor tissue. Although the processing of high-mannose oligosaccharides of a-subunits of heterodimes resembled that of free a-subunits more closely than that of ß-subunits of heterodimers, the differences between the oligosaccharides detected on the two varieties of a-subunits remained substantial enough to suggest that heterodimer formation did affect a-subunit oligosaccharide processing.
Use of subce11ular fractionation techniques disc10sed that combination of a- and ß-subunits began in the rough endop1asmic reticu1um (RER), and combining subunits had high-mannose, endog1ycosidase H-sensitive 01igosaccharides. 143 Interesting1y, combination of LH a- and ß-subunits at very ear1y times of pulse 1abe1ing has been reported also, but subce11u1ar fractionation techniques were not used to isolate RER-associated heterodimers. 141,143 TSH and excess free a-subunits, but no free ß-subunits, were re1eased into the medium after 60 to 240-minutes chase.