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The inclusion of methanol as a constituent of the resolving gel impacted the electrophoretic mobility of proteins across a broad range of molecular masses. There was greater separation of the fast and slow isoforms of human MLC1, as well as separation and high resolution of fast and slow isoforms of the three myosin heavy chain isoforms that are expressed in human skeletal muscle on the same gel format. Furthermore, the same resolving gel format substantially altered the electrophoretic mobility of at least one isoform of tropomyosin in human striated muscle. It is possible that the inclusion of methanol in SDS\u2013PAGE resolving gels could improve the separation of other proteins that are expressed in muscle and in other tissues and cell types.<\/jats:p>","DOI":"10.1002\/elps.202400004","type":"journal-article","created":{"date-parts":[[2024,5,24]],"date-time":"2024-05-24T05:55:28Z","timestamp":1716530128000},"page":"1851-1859","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Methanol gel electrophoresis: Separation of human fast and slow myosin light chain 1 and other myofibrillar protein isoforms on a single gel format"],"prefix":"10.1002","volume":"45","author":[{"given":"Peter J.","family":"Reiser","sequence":"first","affiliation":[{"name":"Division of Biosciences College of Dentistry The Ohio State University  Columbus Ohio 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