Purification and cell-free translation of a unique high molecular weight form of the brain isozyme of creatine phosphokinase from mouse

Eric N. Olson, Brian K. Lathrop, Luis Glaser

Research output: Contribution to journalArticle

3 Scopus citations

Abstract

Mouse brain creatine kinase was purified to homogeneity and shown to consist of two polypeptide chains of 50,000 daltons. This protein thus differs in size from all other creatine kinase molecules purified to data including the mouse muscle enzyme which shows a molecular weight between 39,000 and 42,000. The high molecular weight isozyme has been shown to represent the primary translation product of creatine phosphokinase mRNA from mouse brain. The unusual size of this creatine phosphokinase subunit provides unique tools for the study of the differential regulation of creatine kinase gene expression and for the study of subunit interactions in creatine kinase isozymes.

Original languageEnglish (US)
Pages (from-to)715-723
Number of pages9
JournalBiochemical and Biophysical Research Communications
Volume108
Issue number2
DOIs
StatePublished - Sep 30 1982

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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