Jonscher K R, Yates J R
Department of Molecular Biotechnology, University of Washington, Seattle, Washington 98195-7730, USA.
J Biol Chem. 1997 Jan 17;272(3):1735-41. doi: 10.1074/jbc.272.3.1735.
The polymerase-associated phosphoprotein (P protein) from Sendai virus, a murine Paramyxovirus, is reported in the literature to be a highly phosphorylated protein. In vitro studies have detected phosphorylation in different regions of the protein, while a single phosphopeptide (identified as the sole phosphorylation) site) was observed using in vivo techniques. In this work, two phosphorylation sites of the P protein from Sendai virus are localized by a direct approach using matrix-assisted laser desorption ionization/quadrupole ion trap mass spectrometry. A computer-aided approach is used to confirm peptide identification.
来自仙台病毒（一种鼠副粘病毒）的聚合酶相关磷蛋白（P蛋白）在文献中被报道为一种高度磷酸化的蛋白。体外研究已检测到该蛋白不同区域的磷酸化，而使用体内技术观察到一个单一的磷酸肽（被确定为唯一的磷酸化位点）。在这项工作中，通过使用基质辅助激光解吸电离/四极杆离子阱质谱的直接方法定位了仙台病毒P蛋白的两个磷酸化位点。采用计算机辅助方法来确认肽段鉴定。
