Abstract
Insulin like growth factor (IGF)-1 and IGF-2 were assayed from human plasma via biomolecular interaction analysis mass spectrometry, utilizing antibodies as ligands for affinity retrieval. Detection of both targeted and non-targeted IGFs in the mass spectra indicated possible protein complex retrieval by the individual antibodies. A series of control experiments eliminated the possibility of analyte cross-walking between flow cells, significant antibodies cross-reactivity, and direct IGF interactions. To disrupt the putative protein complex and release its constituent proteins, plasma samples were treated with detergents. An SDS-treated plasma yielded IGF signals in a different ratio than the one observed in the mass spectra from the non-treated plasma, suggesting disruption of the protein complex, and its retrieval from non-treated plasma. Novel truncated IGF-2 variant, missing its N-terminal Alanine, was detected in all mass spectra.
Original language | English (US) |
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Pages (from-to) | 130-134 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 536 |
Issue number | 1-3 |
DOIs | |
State | Published - Feb 11 2003 |
Keywords
- Biomolecular interaction analysis mass spectrometry
- IGF-1
- IGF-2
- Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
- Protein complex
- Surface plasmon resonance
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology