Improved methodology for analysis and quantitation of proteins on one-dimensional silver-stained slab gels
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Age related differences in diaphragm muscle fiber response to mid/long term controlled mechanical ventilation
2014, Experimental GerontologyCitation Excerpt :A muscle fiber was accepted and included in the analyses: (i) if the sarcomere length of a single muscle fiber changed < 0.10 μm between relaxation and maximum activation, (ii) if maximal force changed < 10% from first to seventh activation (Moss, 1979). After mechanical recordings, each skinned fiber was placed in sample buffer (7.43 ml distilled water, 2.1 ml glycerol, 1.4 ml 10% SDS, 1.75 of 0.5 M Tris buffer pH 6.8, 0.32 ml bromophenol blue, 32.4 mg dithiothreitol, 1 ml leupeptin) in a plastic micro-centrifuge tube and stored at − 180 °C for subsequent electrophoretic analysis (Giulian et al., 1983; Larsson et al., 1995). MyHC isoform composition of fibers was then determined by 6% SDS-PAGE (Fig. 1).
Impact of titin isoform on length dependent activation and cross-bridge cycling kinetics in rat skeletal muscle
2013, Biochimica et Biophysica Acta - Molecular Cell ResearchCitation Excerpt :To determine titin isoform expression in both WT and HM TA muscle, TA homogenate samples were suspended in SDS sample buffer and underwent electrophoresis using vertical SDS agarose gels designed for high molecular weight protein separation as described previously [23]. Additionally, to assess the lower molecular weight myofilament protein isoform expression, homogenates samples were separated using standard SDS-PAGE (12%) [24]; gels were stained with Coomassie blue. The compositions of the activating and relaxing solutions were calculated according to the procedures developed by Fabiato as described previously [18].
Human skeletal muscle fiber type specific protein content
2012, Analytical BiochemistryFast and slow muscle fiber transcriptome dynamics with lifelong endurance exercise
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