CiteULike is a free online bibliography manager. Register and you can start organising your references online.

Chemical cleavage at aspartyl residues for protein identification. Export

Analytical chemistry, Vol. 73, No. 22. (15 November 2001), pp. 5395-5402.

Citation Format

[Posts]

View FullText article


robert's tags for this article

cleavage protease protein-analysis proteomics

X Reviews [Write a review of this article]

X Find related articles from these CiteULike users

X Find related articles with these CiteULike tags

X Posting History

X Abstract

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 Tyl-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.


X BibTeX record

X RIS record


Privacy Statement | Terms & Conditions
CiteULike organises scholarly (or academic) papers or literature and provides bibliographic (which means it makes bibliographies) for universities and higher education establishments. It helps undergraduates and postgraduates. People studying for PhDs or in postdoctoral (postdoc) positions. The service is similar in scope to EndNote or RefWorks or any other reference manager like BibTeX, but it is a social bookmarking service for scientists and humanities researchers.