Corder R, Emson P C, Lowry P J
Biochem J. 1984 May 1;219(3):699-706. doi: 10.1042/bj2190699.
Human neuropeptide Y was isolated from acid extracts of adrenal-medullary phaeochromocytoma 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 one leucine residue and its replacement with methionine. 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 methionine to be located at position 17 in human neuropeptide Y.
人神经肽Y是从肾上腺髓质嗜铬细胞瘤组织的酸性提取物中分离出来的。经过硫酸铵分级分离后,从重新溶解的80%饱和度硫酸铵富含肽的沉淀中,通过凝胶过滤、阳离子交换色谱和反相高压液相色谱法纯化出神经肽Y样免疫反应性物质。对该肽进行氨基酸分析,结果显示其组成与猪肽几乎相同,唯一的例外是一个亮氨酸残基缺失,被甲硫氨酸取代。对该肽进行胰蛋白酶消化,随后对片段进行氨基酸分析,进一步证实了该肽的身份。对(1-19)肽胰蛋白酶片段进行羧肽酶Y消化,结果表明甲硫氨酸位于人神经肽Y的第17位。