Conformational and biological properties of di[delta-(5-nitro-2-pyrimidyl)ornithine 17,18]glucagon. Role of the arginine residues.
作者： R M Epand , J J Liepnieks
DOI: 10.1016/S0021-9258(18)33241-1
关键词:
摘要: The reaction of nitromalondialdehyde with the arginine residues glucagon results in conversion 2 peptide to delta-(5-nitro-2-pyrimidyl)ornithine form di[delta-(5-nitro-2-pyrimidyl)ornithine 17,18]glucagon (NP-glucagon). modified does not exhibit any loss ability activate adenylate cyclase rat liver plasma membranes or stimulate glycogenolysis cortisone-primed rabbits relative native hormone despite this marked alteration structure. CD dilute solutions NP-glucagon is similar that hormone. In absence salt, independent concentration, but structures higher helical content are observed concentrated presence 0.1 M NaCl and methanol. extent helix formation under these conditions greater than given by glucagon. Results from viscosity proton magnetic resonance spectra confirm extend previous studies indicate fully active derivative a compact folded conformation.
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