Conformational and biological properties of a covalently linked dimer of glucagon Reaction of mono- and bifunctional sulfenyl halides
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The tryptophan residue of glucagon was modified by reaction with a mono-functional sulfenyl chloride (2-nitrophenylsulfenyl chloride) and with a bifunctional sulfenyl chloride (2,4-dinitro-1,5-phenyldisulfenyl chloride) to produce a monomeric form of glucagon with a modified tryptophan, glucagon-nitrophenylsulfenyl and a dimeric form (glucagon)2-dinitrophenyldisulfenyl respectively. The dimeric form was isolated by chromatography on Sephadex G-50. The circular dichroism spectra of pH and low temperature. The derivatives activated adenylate cyclase from rat liver to an extent comparable to that of the native hormone, indicating that a glucagon dimer is capable of biological activity and that an intact tryptophan residue is not essential for biological response.
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