Mapping of protein phosphorylation by dual enzyme digestion and MALDI/quadrupole orthogonal TOF mass spectrometry

Jun Han, Marshall Pope, Christoph Borchers, Lee M. Graves

Результат исследований: Вклад в конференциюДокументрецензирование

Аннотация

The use of sequential trypsin and proteinase K proteolytic digestion, immobilized metal affinity chromatography (IMAC) and MALDI-qTOFMS for the characterization of protein phosphorylation was discussed. Its utility was tested on a synthetic phosphopeptide and two standard phosphoproteins. It was demonstrated that nonspecific proteinase K could be combined with tryptic digestion and specific IMAC purification to effectively reduce large phosphopeptides to suitable size, which favored MS/MS sequencing and improved the elucidation of protein phosphorylation by MALDI/qTOFMS. It was also found that the process could be used as a supplementary method to facilitate the analysis of large tryptic phosphopeptides that cannot be directly sequenced by MS/MS.

Язык оригиналаАнглийский
Страницы559-560
Число страниц2
СостояниеОпубликовано - 2002
Опубликовано для внешнего пользованияДа
СобытиеProceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics - Orlando, FL, Соединенные Штаты Америки
Продолжительность: 2 июн. 20026 июн. 2002

Конференция

КонференцияProceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics
Страна/TерриторияСоединенные Штаты Америки
ГородOrlando, FL
Период2/06/026/06/02

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