{'fraction_non_alphanumeric': 0.04875717017208413, 'fraction_numerical': 0.017208413001912046, 'mean_word_length': 5.503105590062112, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Enhanced protein electrophoresis technique for separating human skeletal muscle myosin heavy chain isoforms

Talmadge and Roy (J. Appl. Physiol. 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 (IIa, IIx) are not clearly distinguished. 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. MHC specificity of each band was confirmed by Western blot using three monoclonal IgG antibodies (mAbs) immuno‐reactive against MHCI (mAb MHCs, Novacastra Laboratories), MHCI+IIa (mAb BF‐35), and MHCIIa+IIx (mAb SC‐71). Results provide a valuable SDS‐PAGE minigel technique for separating MHC isoforms in human muscle without the difficult task of casting gradient gels.