Selected article for: "identify protein and protein identification"
Author: Ma, Ge; Greenwell-Wild, Teresa; Lei, Kejian; Jin, Wenwen; Swisher, Jennifer; Hardegen, Neil; Wild, Carl T.; Wahl, Sharon M.
Title: Secretory Leukocyte Protease Inhibitor Binds to Annexin II, a Cofactor for Macrophage HIV-1 Infection
  • Document date: 2004_11_15
    • ID: rlabxfss_18
    Snippet: Identification of the SLPI Membrane-binding Protein. To identify such a receptor, macrophage membrane proteins were isolated and SLPI immunoprecipitates were subjected to SDS-PAGE. RhSLPI reproducibly coimmunoprecipitated with protein bands at 36 and ‫24ف‬ kD (Fig. 2 A) , which, being similar to previously described binding activity (3), were selected for further analysis. After in-gel tryptic digestion of these bands, the resultant peptide.....
    Document: Identification of the SLPI Membrane-binding Protein. To identify such a receptor, macrophage membrane proteins were isolated and SLPI immunoprecipitates were subjected to SDS-PAGE. RhSLPI reproducibly coimmunoprecipitated with protein bands at 36 and ‫24ف‬ kD (Fig. 2 A) , which, being similar to previously described binding activity (3), were selected for further analysis. After in-gel tryptic digestion of these bands, the resultant peptides were analyzed by LC-MS/MS and database searching (SEQUEST; Wistar Institute) revealed annexin II as the p36 SLPI-binding partner/receptor. Annexin II was confirmed with monoclonal anti-annexin II and rhSLPI coimmunoprecipitation followed by Western blotting (Fig. 2, B and C) . The p42 SLPI-binding protein band was identified by mass spectrometry as actin, which we determined does not interact with rhSLPI directly, but rather associates with annexin II as part of a trimolecular complex (not depicted).

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