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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)A2株的附着蛋白或G蛋白,并通过反相高效液相色谱(HPLC)分离得到的肽。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)产生质量,对应于带有胞外域的四个Cys残基的残基152-187(残基173、176, 182和186)中的二硫键和不存在糖基化作用。用胃蛋白酶和嗜热菌蛋白酶亚消化该胰蛋白酶消化的肽产生的肽与Cys173和Cys186之间以及Cys176和Cys182之间的二硫键一致。对在MALDI-TOF-MS过程中由消化性肽的源后衰减产生的离子进行的分析显示,肽键断裂且链间二硫键的裂变最小。由这种前所未有的MALDI诱导的源后裂解产生的离子证实了从蛋白水解产物的质量分析推导出的二硫键结构的存在。这些发现表明,G蛋白的胞外域具有一个非糖基化的亚域,其中包含一个“胱氨酸套索”。

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