Massspectrometrical analysis of recombinant human growth hormone Norditropin® reveals amino acid exchange at M14_V14 rhGH
| Autor: | Edina Csaszar, Felix Hepner, Gert Lubec, Elisabeth Roitinger, Arnold Pollak |
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| Rok vydání: | 2006 |
| Předmět: |
Spectrometry
Mass Electrospray Ionization Electrospray ionization Biology Peptide Mapping Biochemistry law.invention law Protein biosynthesis Humans Electrophoresis Gel Two-Dimensional Deamidation Molecular Biology chemistry.chemical_classification Molecular mass Human Growth Hormone Amides Recombinant Proteins Amino acid Molecular Weight Matrix-assisted laser desorption/ionization Amino Acid Substitution chemistry Protein Biosynthesis Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization Codon usage bias Recombinant DNA Chromatography Liquid |
| Zdroj: | PROTEOMICS. 6:775-784 |
| ISSN: | 1615-9861 1615-9853 |
| DOI: | 10.1002/pmic.200500334 |
| Popis: | Recombinant human growth hormone (rhGH) is used for the treatment of several disorders. Structural integrity of rhGH is of critical importance for its clinical use and modifications thereof may act as markers in situations such as rhGH doping, as illegal rhGH-abuse in sports is of increasing interest. In the current study we investigated homogeneity of Norditropin, a recombinant human growth hormone frequently used in medicine, expressed in E. coli, strain MC1061. The most recent proteomics technologies including 2-DE, MALDI-MS followed by MALDI-MS/MS and LC-MS followed by LC-MS/MS were used for the characterisation of rhGH. MALDI-TOF-TOF and electrospray LC-MS analysis revealed one major protein with an average molecular mass of 22 126.0 Da and some additional minor components. Electrospray LC-MS/MS of the enzymatically digested Norditropin sample showed deamidation of N(12)N(149) and N(159), oxidation of M(14), M(125) and M(170) and one amino acid exchange V(14) for M(14) present in |
| Databáze: | OpenAIRE |
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