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"Subunit structure of Escherichia coli exonuclease VII." |
Vales LD, Rabin BA, Chase JW |
Published Aug. 10, 1982 in J Biol Chem volume 257 .
Pubmed ID: 6284744
Abstract:
| Exonuclease VII has been purified 7,500-fold to 87% homogeneity from Escherichia coli K12 using a new purification procedure. The enzyme has been shown to be composed of two nonidentical subunits of 10,500 and 54,000 daltons. This has been confirmed by restoration of exonuclease VII activity after renaturation of denatured and purified subunits. The structure of the native enzyme consists of one large subunit and four small subunits. We have previously isolated exonuclease VII mutant strains containing defects which map at two distinct loci. Subunit-mixing experiments utilizing wild type enzyme and temperature-sensitive enzyme produced by an xseB mutant strain have shown that the xseB gene codes for the small subunit of the enzymes. |
This publication refers to following REPAIRtoire entries:
| Genes | |
| Proteins |
Last modification of this entry: Oct. 6, 2010
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