Synthesis of Escherichia coli branched-chain amino acid aminotransferase in vitro in a coupled transcription-translation system

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Abstract

Synthesis of the Escherichia coli branched-chain amino acid aminotransferase (transaminase-B; EC 2.6.1.42), the product of the ilv E gene, has been accomplished in vitro in a coupled transcription-translation system directed by DNA from a plasmid known to contain the ilv EDA operon. The identification of the protein was determined by its comigration with purified transaminase B, both on two-dimensional gels and on slab gels containing exponential gradients of acrylamide. Also reported is a comparison between RNA-directed and DNA-directed (coupled) protein synthesis reactions for optimal magnesium concentration, pH, template concentration, and kinetics of incorporation.

Original languageEnglish (US)
Pages (from-to)441-448
Number of pages8
JournalAnalytical Biochemistry
Volume105
Issue number2
DOIs
StatePublished - 1980

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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