Improvements in Protein Identification by MALDI-TOF-MS Peptide Mapping

详细信息    查看全文

• 作者：Volker Egelhofer ; Konrad Bü ; ssow ; Christine Luebbert ; Hans Lehrach ; and Eckhard Nordhoff
• 刊名：Analytical Chemistry
• 出版年：2000
• 出版时间：July 1, 2000
• 年：2000
• 卷：72
• 期：13
• 页码：2741 - 2750
• 全文大小：107K
• 年卷期：v.72,no.13(July 1, 2000)
• ISSN：1520-6882

文摘

A new strategy for identifying proteins in sequence databases by MALDI-MS peptide mapping is reported. Thestrategy corrects for systematic deviations of determinedpeptide molecular masses using information contained inthe opened database and thereby renders unnecessaryinternal spectrum calibration. As a result, data acquisitionis simplified and less error prone. Performance of the newstrategy is demonstrated by identification of a set ofrecombinant, human cDNA expression products as wellas native proteins isolated from crude mouse brainextracts by 2-D electrophoresis. Using one set of calibration constants for the mass spectrometric analyses, 20proteins were identified without applying any molecularweight restrictions, which was not possible without datacorrection. A sequence database search program has beenwritten that performs all necessary calculations automatically, access to which will be provided to the scientificcommunity in the Internet.