Peptide mapping analysis of recombinant human interleukin-11 with HPLC-ESI-Q-TOF/MS spectrometry.
- Author:
Ying YANG
1
;
Chun-ming RAO
;
Wei WANG
;
Chun-mei HAN
;
Jun-zhi WANG
Author Information
- Publication Type:Journal Article
- MeSH: Amino Acid Sequence; Chromatography, High Pressure Liquid; methods; Interleukin-11; chemistry; genetics; Molecular Weight; Peptide Fragments; Peptide Mapping; methods; Recombinant Proteins; chemistry; Reproducibility of Results; Spectrometry, Mass, Electrospray Ionization; methods; Tandem Mass Spectrometry; methods
- From: Acta Pharmaceutica Sinica 2006;41(8):756-760
- CountryChina
- Language:Chinese
-
Abstract:
AIMTo analyze the peptide mapping of recombinant human interleukin-11 (rhIL-11) by HPLC-ESI-Q-TOF/MS spectrometry.
METHODSThe trypsin digested rhIL-11 at 37 degrees C over night, and the peptide mapping was performed by HPLC. The relative molecular weight of the peptides fragments was measured by ESI-Q-TOF/MS, and amino acid sequence was analyzed by MS/MS.
RESULTSThe peptide fragments of rhIL-11 in the peptide mapping were assigned by analyzing the retain time, relative molecular weight and amino acid sequence. And 97% of the expected peptides were detected in this way.
CONCLUSIONThe study proves that HPLC-ESI-Q-TOF/MS is a good method to analyze peptide mapping of protein with the advantage of sensitivity, high speed and accuracy.
