{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Malik ZA"],"funding":["NIDDK NIH HHS","NCRR NIH HHS","NIGMS NIH HHS","NIH HHS"],"pagination":["290-308"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3997170"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["1(3)"],"pubmed_abstract":["Two-dimensional gel electrophoresis provides robust comparative analysis of skeletal muscle, but this technique is laborious and limited by its inability to resolve all proteins. In contrast, orthogonal separation by SDS-PAGE and reverse-phase liquid chromatography (RPLC) coupled to mass spectrometry (MS) affords deep mining of the muscle proteome, but differential analysis between samples is challenging due to the greater level of fractionation and the complexities of quantifying proteins based on the abundances of their tryptic peptides. Here we report simple, semi-automated and time efficient (<i>i.e</i>., 3 h per sample) proteome profiling of skeletal muscle by 1-dimensional RPLC electrospray ionisation tandem MS. Solei were analysed from rats (n = 5, in each group) bred as either high"],"journal":["Proteomes"],"pubmed_title":["Label-Free LC-MS Profiling of Skeletal Muscle Reveals Heart-Type Fatty Acid Binding Protein as a Candidate Biomarker of Aerobic Capacity."],"pmcid":["PMC3997170"],"funding_grant_id":["P30 DK020572","R24 OD010950","R01 DK077200","R01 GM104194","R24 RR017718"],"pubmed_authors":["Close GL","Koch LG","Burniston JG","Malik ZA","Britton SL","Cobley JN","Morton JP","Edwards BJ"],"additional_accession":[]},"is_claimable":false,"name":"Label-Free LC-MS Profiling of Skeletal Muscle Reveals Heart-Type Fatty Acid Binding Protein as a Candidate Biomarker of Aerobic Capacity.","description":"Two-dimensional gel electrophoresis provides robust comparative analysis of skeletal muscle, but this technique is laborious and limited by its inability to resolve all proteins. In contrast, orthogonal separation by SDS-PAGE and reverse-phase liquid chromatography (RPLC) coupled to mass spectrometry (MS) affords deep mining of the muscle proteome, but differential analysis between samples is challenging due to the greater level of fractionation and the complexities of quantifying proteins based on the abundances of their tryptic peptides. Here we report simple, semi-automated and time efficient (<i>i.e</i>., 3 h per sample) proteome profiling of skeletal muscle by 1-dimensional RPLC electrospray ionisation tandem MS. Solei were analysed from rats (n = 5, in each group) bred as either high","dates":{"release":"2013-01-01T00:00:00Z","publication":"2013 Dec","modification":"2025-04-19T07:54:20.074Z","creation":"2019-03-27T01:26:57Z"},"accession":"S-EPMC3997170","cross_references":{"pubmed":["24772389"],"doi":["10.3390/proteomes1030290"]}}