[Peptide mapping analysis of recombinant human interleukin-11 with HPLC-ESI-Q-TOF/MS spectrometry].
OBJECTIVE
To analyze the peptide mapping of recombinant human interleukin-11 (rhIL-11) by HPLC-ESI-Q-TOF/MS spectrometry.


METHODS
The 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.


RESULTS
The 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.


CONCLUSIONS
The 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.
Yang
Ying
Y
National Institute for the Control of Pharmaceutical and Biological Products, Beijing 100050, China. y_ying_77@yahoo.com.cn
Rao
Chun-ming
CM
Wang
Wei
W
Han
Chun-mei
CM
Wang
Jun-zhi
JZ
D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid / Q000379:methods*; D017370:Interleukin-11 / Q000737:chemistry* / Q000235:genetics; D008970:Molecular Weight; D010446:Peptide Fragments; D010449:Peptide Mapping / Q000379:methods*; D011994:Recombinant Proteins / Q000737:chemistry; D015203:Reproducibility of Results; D021241:Spectrometry, Mass, Electrospray Ionization / Q000379:methods*; D053719:Tandem Mass Spectrometry / Q000379:methods*
C508611:IL11 protein, human; D017370:Interleukin-11; D010446:Peptide Fragments; D011994:Recombinant Proteins