Resolution of myocardial myosin light chains by two dimensional gel electrophoresis

J. McPherson, R. R. Traut, D. T. Mason, R. Zelis, J. Wikman-Coffelt

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Abstract

Two dimensional gel electrophoresis of canine myocardial light chains of myosin demonstrated the existence of a single polypeptide species corresponding to the lighter component, C 2. However, contrary to previous observations, it was found that the heavier polypeptide, C 1, although homogeneous by one dimensional electrophoresis in polyacrylamide gels containing dodecyl sulfate, is resolved into 4 components by two dimensional gel electrophoresis at pH 8.7 and 4.5. Of these 4 components 2, named C1c and C1d, present in roughly equal amounts, comprise approximately 95% of the total C1 fraction, while the remaining 5% of the C 1 material consists of 2 components, named C1a and C1b.

Original languageEnglish (US)
Pages (from-to)994-996
Number of pages3
JournalJournal of Biological Chemistry
Volume249
Issue number3
StatePublished - 1974

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    McPherson, J., Traut, R. R., Mason, D. T., Zelis, R., & Wikman-Coffelt, J. (1974). Resolution of myocardial myosin light chains by two dimensional gel electrophoresis. Journal of Biological Chemistry, 249(3), 994-996.