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The attachment protein or G protein of the A2 strain of human respiratory syncytial virus (RSV) was digested with trypsin and the resultant peptides separated by reverse-phase high-performance liquid chromatography (HPLC). One tryptic peptide produced a mass by matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) corresponding to residues 152-187 with the four Cys residues of the ectodomain (residues 173, 176, 182, and 186) in disulfide linkage and absence of glycosylation. Sub-digestion of this tryptic peptide with pepsin and thermolysin produced peptides consistent with disulfide bonds between Cys173 and Cys186 and between Cys176 and Cys182. Analysis of ions produced by post-source decay of a peptic peptide during MALDI-TOF-MS revealed fragmentation of peptide bonds with minimal fission of an inter-chain disulfide bond. Ions produced by this unprecedented MALDI-induced post-source fragmentation corroborated the existence of the disulfide arrangement deduced from mass analysis of proteolysis products. These findings indicate that the ectodomain of the G protein has a non-glycosylated subdomain containing a "cystine noose."

译文

用胰蛋白酶消化人呼吸道合胞病毒 (RSV) 的A2菌株的附着蛋白或g蛋白,并通过反相高效液相色谱 (HPLC) 分离所得肽。一种胰蛋白酶肽通过基质辅助激光解吸/电离 (MALDI) 飞行时间 (TOF) 质谱 (MS) 产生了与胞外域的四个Cys残基152-187的残基 (残基173,176,182,和186) 在二硫键连接和不存在糖基化。用胃蛋白酶和嗜热菌素对这种胰蛋白酶进行亚消化,产生的肽与Cys173和Cys186之间以及Cys176和cys182之间的二硫键一致。对maldi-tof-MS期间消化肽的源后衰变产生的离子的分析表明,肽键断裂,链间二硫键的裂变最小。这种前所未有的MALDI诱导的后源断裂产生的离子证实了从蛋白水解产物的质量分析得出的二硫键排列的存在。这些发现表明g蛋白的外结构域具有包含 “胱氨酸套索” 的非糖基化亚域。

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