Methanol gel electrophoresis: Separation of human fast and slow myosin light chain 1 and other myofibrillar protein isoforms on a single gel format.

Autor: Reiser PJ; Division of Biosciences, College of Dentistry, The Ohio State University, Columbus, Ohio, USA., Belevych N; Division of Biosciences, College of Dentistry, The Ohio State University, Columbus, Ohio, USA., Shope L; Division of Biosciences, College of Dentistry, The Ohio State University, Columbus, Ohio, USA., Hanaoka B; Division of Rheumatology and Immunology, Department of Internal Medicine, The Ohio State University, Columbus, Ohio, USA.
Jazyk: angličtina
Zdroj: Electrophoresis [Electrophoresis] 2024 Oct; Vol. 45 (19-20), pp. 1851-1859. Date of Electronic Publication: 2024 May 24.
DOI: 10.1002/elps.202400004
Abstrakt: This report describes a novel sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) resolving gel format that consistently yields the electrophoretic separation of the fast and slow isoforms of human sarcomeric myosin light chain 1 (MLC1). 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-PAGE resolving gels could improve the separation of other proteins that are expressed in muscle and in other tissues and cell types.
(© 2024 The Author(s). ELECTROPHORESIS published by Wiley‐VCH GmbH.)
Databáze: MEDLINE
Externí odkaz: