Functional analysis of cancer-derived immunoglobulin G whole molecule-interacting proteins identified by LC-MS/MS.
- Author:
Ju-Ping WANG
1
;
Han-Ying CHEN
;
Hui PENG
Author Information
- Publication Type:Journal Article
- MeSH: Antibodies, Neoplasm; immunology; Chromatography, Liquid; Electrophoresis, Polyacrylamide Gel; HeLa Cells; Humans; Immunoglobulin G; immunology; Neoplasms; immunology; Proteins; immunology; Tandem Mass Spectrometry
- From: Journal of Southern Medical University 2015;35(1):93-97
- CountryChina
- Language:Chinese
-
Abstract:
OBJECTIVETo identify cancer-derived immunoglobulin G (IgG) whole molecule-interacting proteins to provide important clues for studying IgG biological functions.
METHOSHeLa cell lysate was immunoprecipitated with rabbit antihuman IgG whole molecule antibody and normal rabbit IgG. The immunocomplex underwent sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and was detected with silver staining. Three prominently enhanced bands were subjected to protein identification with liquid chromatography-tandem mass spectrometry (LC-MS/MS), and the MS data were analyzed with Swiss-Prot database. Cancer-derived IgG whole molecule-interacting proteins were screened and functionally annotated.
RESULTS AND CONCLUSIONWe identified 6 potential cancer-derived IgG whole molecule-interacting proteins with co-immunoprecipitation combined with LC-MS/MS, which provides valuable clues for studying the function of cancer-derived IgG.
