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Sequencing of peptides and proteins from the carboxy terminus.
- Source :
-
Analytical biochemistry [Anal Biochem] 1992 Nov 01; Vol. 206 (2), pp. 344-52. - Publication Year :
- 1992
-
Abstract
- A new chemical method for carboxy-terminal (C-terminal) protein sequencing has been developed. This approach has been successfully used to sequence 5 residues of standard proteins and 5 to 10 residues of synthetic peptides at low nanomole levels. The sequencing procedure consists of converting the C-terminal amino acid into a thiohydantoin (TH) derivative, followed by transformation of the TH into a good leaving group by alkylation. Next, the alkylated TH is cleaved mildly and efficiently with (N = C V S)- anion, which simultaneously forms a TH on the newly truncated protein or peptide. Thus, after the initial TH derivatization, there is no return to a free carboxyl group at the C-terminus. An additional benefit of this method is that the alkylating moiety can be chosen with a variety of properties allowing for variation in the detection method. This chemistry has been adapted to automated protein sequencers with a cycle time of about 1 h.
Details
- Language :
- English
- ISSN :
- 0003-2697
- Volume :
- 206
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Analytical biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 1443604
- Full Text :
- https://doi.org/10.1016/0003-2697(92)90376-i