Detection of bound and free IGF‐1 and IGF‐2 in human plasma via biomolecular interaction analysis mass spectrometry
2003; Wiley; Volume: 536; Issue: 1-3 Linguagem: Inglês
10.1016/s0014-5793(03)00042-5
ISSN1873-3468
AutoresDobrin Nedelkov, Randall W. Nelson, Urban A. Kiernan, Eric E. Niederkofler, Kemmons A. Tubbs,
Tópico(s)Erythrocyte Function and Pathophysiology
ResumoInsulin 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.
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