Comparative Purification Of Myocardial Myosin And Antigenic Specificity Of The Two Light Chains

J. Wikman-Coffelt, R. Zelis, C. Fenner, D. T. Mason

Research output: Contribution to journalArticle

33 Scopus citations

Abstract

Dog myocardial myosin preparations, purified according to the procedures presented here, utilizing either one or two (NH4)2SO4fractionations, contained no major contaminants which could be detected by disc gel electrophoresis, and exhibited high myosin ATPase activity. The low molecular weight components (light chains) were dissociated from the rest of the molecule by denaturing with urea; the chains were further purified by column chromatography. Procedures were a modification of those used for purification of skeletal muscle myosin light chains. According to immunoanalyses the two myocardial myosin light chains showed antigenic specificity.

Original languageEnglish (US)
Pages (from-to)439-449
Number of pages11
JournalPreparative Biochemistry
Volume3
Issue number5
DOIs
StatePublished - Jan 1 1973

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Genetics

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