Individual extracted proteins were used in shotgun proteomics analysis with in-gel trypsin digestion followed by tandem mass spectrometry (MS/MS) conducted at the University of Arkansas for Medical Science proteomics core lab (UAMS, Little Rock, AR, USA) [11 (link)]. Raw data were analyzed by database searching using Masco (Matrix Science, Boston, MA, USA) and UniProtKB database (http://www.uniprot.org/help/uniprotkb ) with the result compiled using the Scaffold Program (Proteome Software, Portland, OR, USA).
In Kuttappan et al. [2 (link)], digested sample homogenates were acidified with 1% formic acid, and purified by reversed phase chromatography using C18 affinity media (Omix-Agilent, Santa Clara, CA, USA). Each sample was subjected to three replicate analyses for LC-MS/MS using a hybrid-OrbitrapXL mass spectrometer (ThermoFisher Scientific, Waltham, MA, USA) according to Voruganti et al. [14 (link)]. Mass spectrometry analysis was conducted in the DNA/Protein Resource Facility (Oklahoma State University, Stillwater, OK, USA).
In Kuttappan et al. [2 (link)], digested sample homogenates were acidified with 1% formic acid, and purified by reversed phase chromatography using C18 affinity media (Omix-Agilent, Santa Clara, CA, USA). Each sample was subjected to three replicate analyses for LC-MS/MS using a hybrid-OrbitrapXL mass spectrometer (ThermoFisher Scientific, Waltham, MA, USA) according to Voruganti et al. [14 (link)]. Mass spectrometry analysis was conducted in the DNA/Protein Resource Facility (Oklahoma State University, Stillwater, OK, USA).
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