Abstract
Evidence for conformational differences between precursor and processed forms of thyroid-stimulating hormone beta subunit.
Highlights
The data show that TSHP, as well as the previously identified
A tumor protein about 3000 daltons larger than nonglycosylated TSHa and having tryptic peptides in common with authentic TSHcv was tentatively identified as pre-TSHa [12]. In reports from this laboratory, pre-TSHa was identified immunochemically in translations of mouse tumor mRNA [13, 14], and we have shown it is identical in size to normal mouse pituitary pre-cY
B, to translations of tumor mRNA supplemented with microsomal membranes the following antisera were added: Lane 2, anti-RCM TSHP; Lane 3, antiTSHP; Lane 4, as in Lane 3 with the prior addition of 10 pg of bTSHP; Lane 5, nonimmune serum
Summary
Pre-hCGP was subsequently identified immunochemically with an antiserum to denatured, mature hCGP [6] Precursor forms of both subunits are consistent with the “signal hypothesis” for secreted proteins [18, 19], and partial processing of pre-hCGa by heterologous microsomal membranes recently has been demonstrated [5, 7]. A tumor protein about 3000 daltons larger than nonglycosylated TSHa and having tryptic peptides in common with authentic TSHcv was tentatively identified as pre-TSHa [12] In reports from this laboratory, pre-TSHa was identified immunochemically in translations of mouse tumor mRNA [13, 14], and we have shown it is identical in size to normal mouse pituitary pre-cY [14].
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