PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 3181651-2 1988 Myosin extracted from tumours and electrophoresed on 6%-sodium dodecyl sulfate (SDS)glycerol gels was found to migrate as three distinct MHC components. Sodium Dodecyl Sulfate 80-83 major histocompatibility complex, class I, C Homo sapiens 137-140 2547831-6 1989 By SDS-polyacrylamide gel electrophoresis 2X-MHC shows a lower mobility compared to 2B-MHC and appears to comigrate with 2A-MHC. Sodium Dodecyl Sulfate 3-6 major histocompatibility complex, class I, C Homo sapiens 45-48 32602402-4 2020 The MHC composition was determined using SDS-PAGE. Sodium Dodecyl Sulfate 41-44 major histocompatibility complex, class I, C Homo sapiens 4-7 26842420-1 2016 Single muscle fiber sodium dodecyl sulfate polyacrylamide gel-electrophoresis (SDS-PAGE) is a sensitive technique for determining skeletal muscle myosin heavy chain (MHC) composition of human biopsy samples. Sodium Dodecyl Sulfate 20-42 major histocompatibility complex, class I, C Homo sapiens 166-169 31468173-7 2019 Myosin heavy chain (MHC) isoform was determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Sodium Dodecyl Sulfate 51-73 major histocompatibility complex, class I, C Homo sapiens 0-18 31468173-7 2019 Myosin heavy chain (MHC) isoform was determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Sodium Dodecyl Sulfate 51-73 major histocompatibility complex, class I, C Homo sapiens 20-23 27566374-4 2016 RESULTS: In Young, Middle and Old age groups, by SDS-PAGE MHCI comprised ~1/3 and MHCII ~2/3 of total MHC. Sodium Dodecyl Sulfate 49-52 major histocompatibility complex, class I, C Homo sapiens 58-61 26842420-1 2016 Single muscle fiber sodium dodecyl sulfate polyacrylamide gel-electrophoresis (SDS-PAGE) is a sensitive technique for determining skeletal muscle myosin heavy chain (MHC) composition of human biopsy samples. Sodium Dodecyl Sulfate 79-82 major histocompatibility complex, class I, C Homo sapiens 166-169 23463416-2 2013 The improved technique of SDS-PAGE and 2DE were used to separate porcine MHC isoforms. Sodium Dodecyl Sulfate 26-29 major histocompatibility complex, class I, C Homo sapiens 73-76 25282040-4 2015 Addition of 1500ppm green tea extract was found to modify MHC as evaluated by SDS-PAGE combining both protein staining and specific thiol staining, indicating that protein modifications generated through reactions of green tea phenolic compounds with protein thiols, disrupted the meat emulsion properties leading to reduced water holding capacity and textural stability. Sodium Dodecyl Sulfate 78-81 major histocompatibility complex, class I, C Homo sapiens 58-61 23845398-7 2013 Myosin heavy chain (MHC) isoforms protein and messenger RNA (mRNA) expression were determined with SDS-PAGE (sodium dodecyl sulfate polyacrylamide gel electrophoresis) and RT-PCR (real-time polymerase chain reaction), respectively; IGF-1 (insulin-like growth factor 1), MuRF-1 (muscle RING-finger protein-1), and MAFbx (muscle atrophy f-box) mRNA expression were determined with quantitative RT-PCR. Sodium Dodecyl Sulfate 99-102 major histocompatibility complex, class I, C Homo sapiens 0-18 23845398-7 2013 Myosin heavy chain (MHC) isoforms protein and messenger RNA (mRNA) expression were determined with SDS-PAGE (sodium dodecyl sulfate polyacrylamide gel electrophoresis) and RT-PCR (real-time polymerase chain reaction), respectively; IGF-1 (insulin-like growth factor 1), MuRF-1 (muscle RING-finger protein-1), and MAFbx (muscle atrophy f-box) mRNA expression were determined with quantitative RT-PCR. Sodium Dodecyl Sulfate 99-102 major histocompatibility complex, class I, C Homo sapiens 20-23 23845398-7 2013 Myosin heavy chain (MHC) isoforms protein and messenger RNA (mRNA) expression were determined with SDS-PAGE (sodium dodecyl sulfate polyacrylamide gel electrophoresis) and RT-PCR (real-time polymerase chain reaction), respectively; IGF-1 (insulin-like growth factor 1), MuRF-1 (muscle RING-finger protein-1), and MAFbx (muscle atrophy f-box) mRNA expression were determined with quantitative RT-PCR. Sodium Dodecyl Sulfate 109-131 major histocompatibility complex, class I, C Homo sapiens 0-18 23835800-3 2014 RESULTS: By separation SDS-PAGE-Coomassie and Western blot, only conventional MHC are present. Sodium Dodecyl Sulfate 23-26 major histocompatibility complex, class I, C Homo sapiens 78-81 23463416-5 2013 Major MHC isoforms such as slow, 2a, 2x, and 2b were clearly separated by SDS-PAGE. Sodium Dodecyl Sulfate 74-77 major histocompatibility complex, class I, C Homo sapiens 6-9 23463416-7 2013 Therefore, four MHC isoforms such as slow/I, 2a, 2x, and 2b could be identified by the improved SDS-PAGE technique, 2DE and MS. Sodium Dodecyl Sulfate 96-99 major histocompatibility complex, class I, C Homo sapiens 16-19 22841358-9 2012 Relative expression of MHC proteins was determined by SDS-PAGE electrophoresis. Sodium Dodecyl Sulfate 54-57 major histocompatibility complex, class I, C Homo sapiens 23-26 20060953-6 2010 Myosin heavy chain (MHC) protein isoforms were quantified by silver stained SDS PAGE. Sodium Dodecyl Sulfate 76-79 major histocompatibility complex, class I, C Homo sapiens 0-18 20810908-2 2010 Fiber myosin heavy chain (MHC) isoform content was assayed by SDS-PAGE. Sodium Dodecyl Sulfate 62-65 major histocompatibility complex, class I, C Homo sapiens 26-29 20054086-0 2010 A rationale for SDS-PAGE of MHC isoforms as a gold standard for determining contractile phenotype. Sodium Dodecyl Sulfate 16-19 major histocompatibility complex, class I, C Homo sapiens 28-31 19883388-2 2010 The myosin heavy chain (MHC) isoform distribution of the samples was determined by densitometry of MHC bands separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Sodium Dodecyl Sulfate 122-144 major histocompatibility complex, class I, C Homo sapiens 4-22 19883388-2 2010 The myosin heavy chain (MHC) isoform distribution of the samples was determined by densitometry of MHC bands separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Sodium Dodecyl Sulfate 122-144 major histocompatibility complex, class I, C Homo sapiens 24-27 19883388-2 2010 The myosin heavy chain (MHC) isoform distribution of the samples was determined by densitometry of MHC bands separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Sodium Dodecyl Sulfate 181-184 major histocompatibility complex, class I, C Homo sapiens 4-22 19883388-2 2010 The myosin heavy chain (MHC) isoform distribution of the samples was determined by densitometry of MHC bands separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Sodium Dodecyl Sulfate 181-184 major histocompatibility complex, class I, C Homo sapiens 24-27 16644798-6 2006 Using a SDS-PAGE protocol that proved successful with mammalian muscle MHC isoforms, we were able to detect five MHC isoforms in Xenopus iliofibularis muscle. Sodium Dodecyl Sulfate 8-11 major histocompatibility complex, class I, C Homo sapiens 71-74 18978449-13 2008 Mixed MHC isoform distribution was confirmed by SDS-PAGE, which also indicated that the IIa and IIx isoforms were roughly equally present across the muscles. Sodium Dodecyl Sulfate 48-51 major histocompatibility complex, class I, C Homo sapiens 6-9 18787035-5 2008 Consistent with these results, SDS-PAGE analysis revealed significantly elevated expression of alpha myosin heavy chain (MHC) isoform in epicardial fibres (13 +/- 1%) versus endocardial fibres (3 +/- 1%). Sodium Dodecyl Sulfate 31-34 major histocompatibility complex, class I, C Homo sapiens 101-119 18787035-5 2008 Consistent with these results, SDS-PAGE analysis revealed significantly elevated expression of alpha myosin heavy chain (MHC) isoform in epicardial fibres (13 +/- 1%) versus endocardial fibres (3 +/- 1%). Sodium Dodecyl Sulfate 31-34 major histocompatibility complex, class I, C Homo sapiens 121-124 16644798-6 2006 Using a SDS-PAGE protocol that proved successful with mammalian muscle MHC isoforms, we were able to detect five MHC isoforms in Xenopus iliofibularis muscle. Sodium Dodecyl Sulfate 8-11 major histocompatibility complex, class I, C Homo sapiens 113-116 15731398-8 2005 MHC isoform composition was determined with SDS-PAGE. Sodium Dodecyl Sulfate 44-47 major histocompatibility complex, class I, C Homo sapiens 0-3 16823344-7 2006 MHC isoform composition was determined by SDS-PAGE. Sodium Dodecyl Sulfate 42-45 major histocompatibility complex, class I, C Homo sapiens 0-3 16533350-4 2006 SDS-polyacrylamide electrophoresis revealed in single fibers that the number of fibers expressing myosin heavy chain (MHC) type I isoform decreased from 68.7% to 60.9% (P<0.05), MHC I/IIA isoform was unaltered, while MHC IIA fibers increased from 21.6% to 35.7% and the 4.8% MHC IIA/IIX disappeared with the training (both P<0.05). Sodium Dodecyl Sulfate 0-3 major histocompatibility complex, class I, C Homo sapiens 98-116 16533350-4 2006 SDS-polyacrylamide electrophoresis revealed in single fibers that the number of fibers expressing myosin heavy chain (MHC) type I isoform decreased from 68.7% to 60.9% (P<0.05), MHC I/IIA isoform was unaltered, while MHC IIA fibers increased from 21.6% to 35.7% and the 4.8% MHC IIA/IIX disappeared with the training (both P<0.05). Sodium Dodecyl Sulfate 0-3 major histocompatibility complex, class I, C Homo sapiens 118-121 15621050-6 2005 MHC isoform composition was determined by one-dimensional SDS-gel electrophoresis. Sodium Dodecyl Sulfate 58-61 major histocompatibility complex, class I, C Homo sapiens 0-3 15877992-7 2005 Myosin heavy chain (MHC) composition was assessed using sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Sodium Dodecyl Sulfate 56-78 major histocompatibility complex, class I, C Homo sapiens 0-18 12784168-5 2003 MHC isoform was analyzed by SDS-PAGE using silver stain and MHC isoform mRNA by RT-PCR. Sodium Dodecyl Sulfate 28-31 major histocompatibility complex, class I, C Homo sapiens 0-3 9843753-1 1998 Using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), we have developed a simple method to isolate myosin heavy chain (MHC) and actin from small (60-80 mg) human skeletal muscle samples for the determination of their fractional synthesis rates. Sodium Dodecyl Sulfate 65-68 major histocompatibility complex, class I, C Homo sapiens 121-139 12402179-3 2002 SDS-PAGE of single muscle fibers revealed a higher proportion of MHC I in DIST compared to MID and REC (74.9 +/- 4.3 vs 54.4 +/- 2.8 vs 56.2 +/- 2.9 %, respectively; p < 0.05), less MHC IIa/IIx in DIST compared to MID and REC (0.0 +/- 0.0 vs 6.0 +/- 2.4 vs 15.9 +/- 4.2 %, respectively; p < 0.05), and more total hybrids (I/IIa+IIa/IIx+I/IIa/IIx) in REC than both run groups, DIST and MID (23.0 +/- 3.3 vs 6.2 +/- 1.1 vs 13.2 +/- 2.6 %, respectively; p < 0.05). Sodium Dodecyl Sulfate 0-3 major histocompatibility complex, class I, C Homo sapiens 65-68 12402179-3 2002 SDS-PAGE of single muscle fibers revealed a higher proportion of MHC I in DIST compared to MID and REC (74.9 +/- 4.3 vs 54.4 +/- 2.8 vs 56.2 +/- 2.9 %, respectively; p < 0.05), less MHC IIa/IIx in DIST compared to MID and REC (0.0 +/- 0.0 vs 6.0 +/- 2.4 vs 15.9 +/- 4.2 %, respectively; p < 0.05), and more total hybrids (I/IIa+IIa/IIx+I/IIa/IIx) in REC than both run groups, DIST and MID (23.0 +/- 3.3 vs 6.2 +/- 1.1 vs 13.2 +/- 2.6 %, respectively; p < 0.05). Sodium Dodecyl Sulfate 0-3 major histocompatibility complex, class I, C Homo sapiens 185-188 11740293-5 2001 Expression of MHC isoforms was determined by SDS-PAGE. Sodium Dodecyl Sulfate 45-48 major histocompatibility complex, class I, C Homo sapiens 14-17 11401296-1 2001 We have developed a new method that provides enhanced resolution of myosin heavy chain (MHC) isoforms by sodium dodecyl sulfate--polyacrylamide gel electrophoresis (SDS-PAGE). Sodium Dodecyl Sulfate 105-127 major histocompatibility complex, class I, C Homo sapiens 88-91 11401296-1 2001 We have developed a new method that provides enhanced resolution of myosin heavy chain (MHC) isoforms by sodium dodecyl sulfate--polyacrylamide gel electrophoresis (SDS-PAGE). Sodium Dodecyl Sulfate 165-168 major histocompatibility complex, class I, C Homo sapiens 88-91 10975839-0 2000 Beta 57-Asp plays an essential role in the unique SDS stability of HLA-DQA1*0102/DQB1*0602 alpha beta protein dimer, the class II MHC allele associated with protection from insulin-dependent diabetes mellitus. Sodium Dodecyl Sulfate 50-53 major histocompatibility complex, class I, C Homo sapiens 130-133 10975839-1 2000 Studies of the stability of HLA-DQ have revealed a correlation between SDS stability of MHC class II alphabeta dimers and insulin-dependent diabetes mellitus (IDDM) susceptibility. Sodium Dodecyl Sulfate 71-74 major histocompatibility complex, class I, C Homo sapiens 88-91 10975839-2 2000 The MHC class II alphabeta dimer encoded by HLA-DQA1*0102/DQB1*0602 (DQ0602), which is a dominant protective allele in IDDM, exhibits the greatest SDS stability among HLA-DQ molecules in EBV-transformed B-lymphoblastoid cells and PBLs. Sodium Dodecyl Sulfate 147-150 major histocompatibility complex, class I, C Homo sapiens 4-7 10526246-4 1999 METHODS: MHC isoform composition in biopsies obtained from the vastus lateralis muscle was determined using SDS-PAGE. Sodium Dodecyl Sulfate 108-111 major histocompatibility complex, class I, C Homo sapiens 9-12 9843753-1 1998 Using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), we have developed a simple method to isolate myosin heavy chain (MHC) and actin from small (60-80 mg) human skeletal muscle samples for the determination of their fractional synthesis rates. Sodium Dodecyl Sulfate 6-28 major histocompatibility complex, class I, C Homo sapiens 121-139 12672369-4 2003 MHC composition was determined via SDS gel electrophoresis and quantified using a scanning and densometric system. Sodium Dodecyl Sulfate 35-38 major histocompatibility complex, class I, C Homo sapiens 0-3 10217154-3 1999 1993, 75, 2337-2340) previously established a sodium dodecyl sulfate - polyacrylamide gel electrophoresis (SDS-PAGE) protocol for separating all four rat skeletal muscle myosin heavy chain (MHC) isoforms (MHC I, IIa, IIx, IIb); however, when applied to human muscle, the type II MHC isoforms (Ila, IIx) are not clearly distinguished. Sodium Dodecyl Sulfate 46-68 major histocompatibility complex, class I, C Homo sapiens 190-193 10217154-3 1999 1993, 75, 2337-2340) previously established a sodium dodecyl sulfate - polyacrylamide gel electrophoresis (SDS-PAGE) protocol for separating all four rat skeletal muscle myosin heavy chain (MHC) isoforms (MHC I, IIa, IIx, IIb); however, when applied to human muscle, the type II MHC isoforms (Ila, IIx) are not clearly distinguished. Sodium Dodecyl Sulfate 107-110 major histocompatibility complex, class I, C Homo sapiens 190-193 10217154-4 1999 In this brief paper we describe a modification of the SDS-PAGE protocol which yields distinct and consistent separation of all three adult human MHC isoforms (MHC I, IIa, IIx) in a minigel system. Sodium Dodecyl Sulfate 54-57 major histocompatibility complex, class I, C Homo sapiens 145-148 10217154-4 1999 In this brief paper we describe a modification of the SDS-PAGE protocol which yields distinct and consistent separation of all three adult human MHC isoforms (MHC I, IIa, IIx) in a minigel system. Sodium Dodecyl Sulfate 54-57 major histocompatibility complex, class I, C Homo sapiens 159-162 10217154-6 1999 Results provide a valuable SDS-PAGE minigel technique for separating MHC isoforms in human muscle without the difficult task of casting gradient gels. Sodium Dodecyl Sulfate 27-30 major histocompatibility complex, class I, C Homo sapiens 69-72 9843753-1 1998 Using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), we have developed a simple method to isolate myosin heavy chain (MHC) and actin from small (60-80 mg) human skeletal muscle samples for the determination of their fractional synthesis rates. Sodium Dodecyl Sulfate 65-68 major histocompatibility complex, class I, C Homo sapiens 141-144 9710860-3 1998 The MHC composition of muscle homogenates was determined by electrophoresis techniques (SDS-PAGE). Sodium Dodecyl Sulfate 88-91 major histocompatibility complex, class I, C Homo sapiens 4-7 9242718-2 1997 Subsequently, the isoforms of the myosin heavy chain (MHC) were analysed by sodium dodecyl sulphate (SDS) gel electrophoresis. Sodium Dodecyl Sulfate 76-99 major histocompatibility complex, class I, C Homo sapiens 34-52 9518724-8 1998 Single fibre analysis using SDS-PAGE revealed that MHCs from immunohistochemically defined type 1, type 2 and type 3 fibres ran as three distinct isoform bands, while MHC of tonic fibres co-migrated with type 1 MHC. Sodium Dodecyl Sulfate 28-31 major histocompatibility complex, class I, C Homo sapiens 51-54 9575870-4 1998 Myosin was characterized with electrophoresis in nondenaturing conditions, SDS-glycerol PAGE, and Western blotting with monoclonal antibodies specific for slow and fast myosin heavy chain (MHC) isoforms. Sodium Dodecyl Sulfate 75-78 major histocompatibility complex, class I, C Homo sapiens 189-192 9242718-2 1997 Subsequently, the isoforms of the myosin heavy chain (MHC) were analysed by sodium dodecyl sulphate (SDS) gel electrophoresis. Sodium Dodecyl Sulfate 76-99 major histocompatibility complex, class I, C Homo sapiens 54-57 9242718-2 1997 Subsequently, the isoforms of the myosin heavy chain (MHC) were analysed by sodium dodecyl sulphate (SDS) gel electrophoresis. Sodium Dodecyl Sulfate 101-104 major histocompatibility complex, class I, C Homo sapiens 34-52 9242718-2 1997 Subsequently, the isoforms of the myosin heavy chain (MHC) were analysed by sodium dodecyl sulphate (SDS) gel electrophoresis. Sodium Dodecyl Sulfate 101-104 major histocompatibility complex, class I, C Homo sapiens 54-57 9224541-7 1997 MHC protein isoform differences were determined through sodium dodecyl-polyacrylamide gel electrophoresis (SDS-PAGE) followed by densitometric analysis. Sodium Dodecyl Sulfate 107-110 major histocompatibility complex, class I, C Homo sapiens 0-3 8253204-1 1993 At least four myosin heavy chain (MHC) isoforms were separated by SDS-PAGE in extracts of intrafusal fibers isolated by microdissection from human lumbrical muscles. Sodium Dodecyl Sulfate 66-69 major histocompatibility complex, class I, C Homo sapiens 34-37 8498577-1 1993 Two smooth muscle myosin heavy chains (MHC; SM1 and SM2) of approximately 204 and 200 kDa exist in smooth muscle cells and can be visualized on reducing sodium dodecyl sulfate (SDS)-polyacrylamide gels. Sodium Dodecyl Sulfate 153-175 major histocompatibility complex, class I, C Homo sapiens 39-42 8498577-1 1993 Two smooth muscle myosin heavy chains (MHC; SM1 and SM2) of approximately 204 and 200 kDa exist in smooth muscle cells and can be visualized on reducing sodium dodecyl sulfate (SDS)-polyacrylamide gels. Sodium Dodecyl Sulfate 177-180 major histocompatibility complex, class I, C Homo sapiens 39-42 8621918-5 1996 Results of T cell stimulation studies were correlated with two well studied characteristics of the peptide/MHC complex, which are the affinity of peptide binding to MHC and the stability of the resulting complex upon PAGE in the presence of SDS. Sodium Dodecyl Sulfate 241-244 major histocompatibility complex, class I, C Homo sapiens 107-110 8543946-7 1995 Myosin heavy chain (MHC) and light chain (MLC) isoforms were resolved by 6% and 12% sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE), respectively, and quantified densitometrically. Sodium Dodecyl Sulfate 84-107 major histocompatibility complex, class I, C Homo sapiens 0-18 8543946-7 1995 Myosin heavy chain (MHC) and light chain (MLC) isoforms were resolved by 6% and 12% sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE), respectively, and quantified densitometrically. Sodium Dodecyl Sulfate 144-147 major histocompatibility complex, class I, C Homo sapiens 0-18 7864081-2 1995 Separation and detection of MHCs by sodium dodecyl sulfate-polyacrylamide gel electrophoresis were achieved to a degree such that MHC composition is consistent with previous reports on functional and mRNA data. Sodium Dodecyl Sulfate 36-58 major histocompatibility complex, class I, C Homo sapiens 28-31 7836942-9 1994 Even in biopsies that contained relatively large amounts of these last three fibre types, the amount of neonatal and/or alpha-cardiac MHC detected on SDS-PAGE was limited, suggesting that these MHCs are a minor component in the fibres in which they are expressed. Sodium Dodecyl Sulfate 150-153 major histocompatibility complex, class I, C Homo sapiens 134-137