Optimization of guanidination procedures for MALDI mass mapping

Optimization of guanidination procedures for MALDI mass mapping
复制标题

DOI:
10.1021/ac015613o
复制
发表时间:
2002-04-15
影响因子:
7.4
通讯作者:
Reilly, JP
Reilly, JP
中科院分区:
化学1区
文献类型:
--
作者:
Beardsley, RL;Reilly, JP

文献摘要

被引文献

相似文献

改进的程序胍含赖氨酸的肽,衍生化,结果在增加MALDI质谱信号强度。赖氨酸的完全转换为homoacetylines可以在短短5分钟内完成。该方法被证明在一个模型肽和胰蛋白酶消化的三种蛋白质。为了证明对蛋白质组学样品的适用性,将其成功应用于50 fmol蛋白质的消化。对胍基化后低量蛋白酶的浓缩和纯化方法进行了评价。使用模型肽GRGDSPK的实验使得能够研究胍化反应的特异性。
Improved procedures for guanidination of lysine-containing peptides, a derivatization that results in increased MALDI mass spectral signal intensities are presented. The complete conversion of lysines to homoarginines can be accomplished in as little as 5 min. The method is demonstrated on a model peptide and on tryptic digests of three proteins. To demonstrate the applicability to proteomics samples, it is successfully applied to the digest of 50 fmol of a protein. Approaches for concentrating and purifying low-quantity protein digests following guanidination are evaluated. Experiments with the model peptide GRGDSPK enable investigation of the specificity of the guanidination reaction.