作者: Hidetsugu Fujigaki , Mitsuru Seishima , Kuniaki Saito
DOI: 10.1007/S00216-012-5946-2
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摘要: Protein posttranslational modifications (PTMs) perform essential roles in the biological regulation of a cell. PTMs are extremely important because they can change protein’s physical or chemical properties, conformation, activity, cellular location, stability. In fact, most proteins altered by addition removal moiety on either an amino acid N- C-terminus. Some be added and removed dynamically as mechanism for reversibly controlling protein function. Thus, identifying PTM sites is critical to fully understand any given protein. Mass spectrometry (MS) widely used analytical strategy identify PTMs. We have automated two-dimensional liquid chromatography (LC) system coupled with electrospray ionization quadrupole ion-trap MS indoleamine 2,3-dioxygenase 1 (IDO1), one tryptophan catabolic enzymes. IDO1 promotes immune tolerance suppressing local T-cell responses under various physiological pathophysiological conditions, such pregnancy mammals, tumor resistance, autoimmunity, chronic inflammation. Although many studies demonstrated importance IDO enzymes remain largely unknown. Only few been found, nitration, N-terminal acetylation, phosphorylation. this review, we analyze using our LC-MS/MS system, provide overview current understanding.