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Retention of enzymatic activity by N-terminal domain (1-78) T4-lysozyme: expression of synthetic DNA in Escherichia coli.

From National Research Council Canada

DOIResolve DOI: https://doi.org/10.1016/0006-291x(87)91305-2
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FormatText, Article
Abstract
DNA of 235 b.p. coding for N-terminal domain (1-78) T4-lysozyme was synthesized and cloned by ligating twelve synthetic fragments with a linearized plasmid pUCE8 followed by transformation. On expression in E. coli strain JM103 cells, colonies containing the synthetic DNA were found to be lytic. On purification, clone ptly. 23-5 was found to contain polypeptide (M.W. 10,500), corresponding to N-terminal domain, its dimeric and aggregate form. It was identified by amino acid sequence analysis of the dimeric form.
Publication date
PublisherElsevier
In
  • Biochemical and Biophysical Research Communications 145, no. 1: 190–195.
LanguageEnglish
Peer reviewedYes
NRC numberPHIPPS1987
NPARC number9360772
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Record identifier8e65f2f7-96e4-4535-b5a5-08d829801a8b
Record created2009-07-10
Record modified2020-03-17
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