Peptide-mass profiles of polyvinylidene difluoride-bound proteins by matrix-assisted laser desorption ionization time-of-flight mass spectrometry in the presence of nonionic detergents
Peptide-mass profiles of polyvinylidene difluoride-bound proteins by matrix-assisted laser desorption ionization time-of-flight mass spectrometry in the presence of nonionic detergents
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DOI：
10.1006/abio.1996.0012
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发表时间：
1996-01-01
影响因子：
2.9
通讯作者：
Mische, SM
中科院分区：
文献类型：
--
作者：
Gharahdaghi, F;Kirchner, M;Mische, SM
基质辅助激光解吸/电离飞行时间质谱（MALDI-TOF MS）结合蛋白质的酶消化和肽质量数据库的分子量搜索是用于肽/蛋白质鉴定的强有力的技术。理想情况下，肽混合物应与MALDI-TOF和微测序兼容。在我们的实验室中，在非离子洗涤剂的存在下，从聚偏二氟乙烯（PVDF）结合的蛋白质中进行酶消化和提取肽。然而，非离子去污剂已显示在MALDI-TOF分析中引起信号抑制。本研究表明，通过使用改性的基质溶液，通过MALDI-TOF的PVDF结合蛋白质的肽质量指纹图谱可以在非离子去污剂如氢化Triton X-100（RTX-100），辛基吡喃葡萄糖苷和吐温20的存在下获得。(C)出版社：Academic Press，Inc.
Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS), in conjunction with enzymatic digestion of proteins and molecular weight search of peptide-mass database is a powerful technique for peptide/protein identification. Ideally, peptide mixtures should be compatible with both MALDI-TOF and microsequencing. In our laboratory, enzymatic digestion and extraction of peptides from polyvinylidene difluoride (PVDF)bound proteins is performed in the presence of nonionic detergents. However, nonionic detergents have been shown to cause signal suppression in MALDI-TOF analysis. This study demonstrates that by using a modified matrix solution, peptide-mass fingerprinting of PVDF-bound proteins by MALDI-TOF can be obtained in the presence of nonionic detergents such as hydrogenated Triton X-100 (RTX-100), octylglucopyranoside, and Tween 20. (C) 1996 Academic Press, Inc.