Purification and characterization of human neuropeptide Y from adrenal-medullary phaeochromocytoma tissue

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Abstract
Human neuropeptide Y was isolated from acid extracts of adrenal-medullary pheochromocytoma tissue. After (NH4)2SO4 fractionation, the neuropeptide Y-like immunoreactivity was purified from the resolubilized 80%-saturation-(NH4)2SO4 peptide-rich precipitate, by gel filtration, cation-exchange chromatography and reverse-phase high-pressure liquid chromatography. Amino acid analysis of the peptide revealed a composition almost identical with that of the pig peptide, the exception being the loss of 1 Leu residue and its replacement with Met. Tryptic digestion of the peptide and subsequent amino acid analysis of the fragments further confirmed the identity of the peptide. Carboxypeptidase Y digestion of the (1-19)-peptide tryptic fragment has shown the Met to be located at position 17 in human neuropeptide Y.