Measurement of the amino acid sequence for the fusion protein FP3 with LC-MS/MS.
- Author:
Xiang LI
;
Xiangdong GAO
;
Lei TAO
;
Dening PEI
;
Ying GUO
;
Chunming RAO
;
Junzhi WANG
- Publication Type:Journal Article
- From:
Acta Pharmaceutica Sinica
2012;47(2):216-22
- CountryChina
- Language:Chinese
-
Abstract:
The amino acid sequence of the fusion protein FP3 was measured by two types of LC-MS/MS and its primary structure was confirmed. After reduction and alkylation, the protein was digested with trypsin and glycosyl groups in glycopeptide were removed by PNGase F. The mixed peptides were separated by LC, then Q-TOF and Ion trap tandem mass spectrometry were used to measure b, y fragment ions of each peptide to analyze the amino acid sequence of fusion protein FP3. Seventy-six percent of full amino acid sequence of the fusion protein FP3 was measured by LC-ESI-Q-TOF with the remaining 24% completed by LC-ESI-Trap. As LC-MS and tandem mass spectrometry are rapid, sensitive, accurate to measure the protein amino acid sequence, they are important approach to structure analysis and identification of recombinant protein.
