Resolution of myocardial myosin light chains by two dimensional gel electrophoresis

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

Research output: Contribution to journalArticlepeer-review

14 Scopus citations

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, C2. However, contrary to previous observations, it was found that the heavier polypeptide, C1, 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 C1 material consists of 2 components, named C1a and C1b.

Original languageEnglish (US)
Pages (from-to)994-996
Number of pages3
JournalUnknown Journal
Volume249
Issue number3
StatePublished - 1974

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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