Selected article for: "formic acid and mass spectrometer"
Author: Joshi, Shilvi; Chen, Lang; Winter, Michael B.; Lin, Yi-Lun; Yang, Yang; Shapovalova, Mariya; Smith, Paige M.; Liu, Chang; Li, Fang; LeBeau, Aaron M.
Title: The Rational Design of Therapeutic Peptides for Aminopeptidase N using a Substrate-Based Approach
  • Document date: 2017_5_2
    • ID: 0pmo3opx_23
    Snippet: MSP-MS assays were carried out as described previously 16 . Briefly, 0.2 µg/mL recombinant human APN from R&D Systems (catalog #: 3815-ZN-010) and matched no-enzyme control were assayed against a diverse library of 228 tetradecapeptides pooled at 500 nM in D-PBS (pH 7.4) containing 1 mM TCEP. After 1, 15, 60, 240, and 1200 min, 30 µL of assay mixture was removed, quenched with 7.5 µL 20% formic acid, and flash-frozen in liquid N 2 . Prior to m.....
    Document: MSP-MS assays were carried out as described previously 16 . Briefly, 0.2 µg/mL recombinant human APN from R&D Systems (catalog #: 3815-ZN-010) and matched no-enzyme control were assayed against a diverse library of 228 tetradecapeptides pooled at 500 nM in D-PBS (pH 7.4) containing 1 mM TCEP. After 1, 15, 60, 240, and 1200 min, 30 µL of assay mixture was removed, quenched with 7.5 µL 20% formic acid, and flash-frozen in liquid N 2 . Prior to mass spectrometry acquisition, peptide samples were desalted using C 18 desalting tips and rehydrated in 0.2% formic acid. LC-MS/ MS data were acquired using a Thermo Scientific LTQ-FT mass spectrometer, which was equipped with a Thermo Scientific EASY-Spray Ion Source, EASY-Spray PepMap C 18 Column (3 µM, 100 Å), and Waters nanoACQUITY UPLC System.

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