Conformational and biological properties of a covalently linked dimer of glucagon. Reaction of mono- and bifunctional sulfenyl halides.
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.
D000262:Adenylyl Cyclases / Q000378:metabolism; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001665:Binding Sites; D001681:Biological Assay; D002942:Circular Dichroism; D005934:Glucagon / Q000494:pharmacology; D005947:Glucose / Q000378:metabolism; D008099:Liver / Q000187:drug effects; D046911:Macromolecular Substances; D008297:Male; D011485:Protein Binding; D011487:Protein Conformation; D051381:Rats; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D013434:Sulfenic Acids / Q000494:pharmacology; D014364:Tryptophan
D000596:Amino Acids; D046911:Macromolecular Substances; D013434:Sulfenic Acids; D014364:Tryptophan; D005934:Glucagon; D000262:Adenylyl Cyclases; D005947:Glucose