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Separation of Functional and Non-functional β Subunits of Thyrotropin Preparations by Polyacrylamide Gel Electrophoresis¹

Department of Biological Chemistry, UCLA School of Medicine Los Angeles, California 90024

Abstract

Electrophoretic patterns of intact human and bovine TSH and bovine LH can be clearly distinguished from those of their subunits in 12% polyacrylamide gels, thus providing an easy method of examining subunit recombination. Two distinct components of both bovine and human TSH-β subunits are observed, of which only one recombines with a subunits. Both β-components crossreact with antisera to TSH and TSH-β and have, within experimental error, identical amino acid compositions. Thus, the non-recombining component is a non-functional form of TSH-β which has retained its immunological specificity, and the data explain why the recovery of biological activity during the recombination of TSH subunits is substantially less than with several other glycoprotein hormone preparations.

Footnotes

¹ Supported in part by United States Public Health Service grant AM 18005 and Training Grant GM 00364.

Received March 17, 1977.