CHARACTERIZATION OF PEPTIDES BOUND TO THE CLASS-I MHC MOLECULE HLA-A2.1 BY MASS-SPECTROMETRY
CHARACTERIZATION OF PEPTIDES BOUND TO THE CLASS-I MHC MOLECULE HLA-A2.1 BY MASS-SPECTROMETRY
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DOI：
10.1126/science.1546328
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发表时间：
1992-03-06
期刊：
影响因子：
56.9
通讯作者：
ENGELHARD, VH
中科院分区：
文献类型：
--
作者：
HUNT, DF;HENDERSON, RA;ENGELHARD, VH
由T细胞识别的抗原表达为与主要组织相容性复合体（MHC）分子结合的肽。采用微毛细管高效液相色谱-电喷雾电离-串联质谱法对从MHC分子HLA-A2.1中分离的亚皮摩尔量的肽进行分离和测序。在定量的200种不同物种中，有8种被测序，4种在细胞蛋白中被发现。所有的都是9个残基长，并共享一个独特的结构基序。这种方法的灵敏度和速度应该增强对来自少量病毒感染和转化细胞以及与自身免疫性疾病状态相关的细胞的肽的分析。
Antigens recognized by T cells are expressed as peptides bound to major histocompatibility complex (MHC) molecules. Microcapillary high-performance liquid chromatography - electrospray ionization-tandem mass spectrometry was used to fractionate and sequence subpicomolar amounts of peptides isolated from the MHC molecule HLA-A2.1. Of 200 different species quantitated, eight were sequenced and four were found in cellular proteins. All were nine residues long and shared a distinct structural motif. The sensitivity and speed of this approach should enhance the analysis of peptides from small quantities of virally infected and transformed cells as well as those associated with autoimmune disease states.