Chemical cleavage at aspartyl residues for protein identification

被引:116
作者
Li, AQ
Sowder, RC
Henderson, LE
Moore, SP
Garfinkel, DJ
Fisher, RJ
机构
[1] NCI, SAIC Frederick, Prot Chem Lab, AIDS Vaccine Program, Frederick, MD 21702 USA
[2] NCI, SAIC Frederick, Gene Regulat & Chromosome Biol Lab, Frederick, MD 21702 USA
关键词
D O I
10.1021/ac010619z
中图分类号
O65 [分析化学];
学科分类号
070302 ; 081704 ;
摘要
An alternative method to enzymatic digestion for protein identification by mass spectrometry has been developed that is based on chemical cleavage by formic acid. This method was tested on gel-purified apomyoglobin and BSA, as well as unknown proteins that cofractionate with Ty1-virus-like particles from Saccharomyces cerevisiae. Cleavage at aspartyl residues was found to be efficient and specific, and this specificity of cleavage lent itself easily to database searches. Parallel digestions using trypsin were also performed. The formic acid cleavage method generated comparable or better results than tryptic digestion for protein identification.
引用
收藏
页码:5395 / 5402
页数:8
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