Abstract:The alpha subunit of ovine lutropin can be nicked with the endoproteinase Arg-C to give a single cleavage of the Arg46-Ser47 peptide bond. Following reduction by sulfitolysis, the N-terminal (residues 1-46) and C-terminal (residues 47-96) fragments can be separated and then recombined and reoxidized to yield a reconstituted nicked alpha that binds to the beta subunit but exhibits only 2-3% of the receptor-binding potency of intact lutropin. We have investigated nicked alpha, the two separated fragments, and re… Show more
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