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© Institut Pasteur
Cristaux de cellulase, enzyme purifiée de Clostridium thermocellum permettant la digestion de la cellulose. Image colorisée.
Publication : European journal of biochemistry / FEBS

Preparation and use of a universal primed Sepharose for the purification of DNA-binding proteins

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in European journal of biochemistry / FEBS - 01 Feb 1989

Arcangioli B, Pochet S, Sousa R, Huynh-Dinh T

Link to Pubmed [PMID] – 2645138

Eur. J. Biochem. 1989 Feb;179(2):359-63

We have devised a novel method for the construction of a DNA affinity matrix and tested its use in the purification of a sequence-specific DNA-binding protein from the yeast Saccharomyces cerevisiae. The matrix was prepared in two steps: first, a palindromic oligonucleotide containing an XhoI cohesive end was covalently linked via its loop to a Sepharose matrix; second, directly to this ‘universal’ primed Sepharose was ligated a 37-bp oligonucleotide, with XhoI cohesive ends, containing the sequence of the upstream activation sequence 1 (UAS1) site of the yeast iso-1-cytochrome c (CYC1) gene. After fractionating a yeast crude extract through DEAE-cellulose, heparin ultrogel and Mono Q columns, a single pass through the affinity matrix allowed the purification to apparent homogeneity of the 120-kDa protein factor P, which is responsible for the binding to the UAS1 site.

http://www.ncbi.nlm.nih.gov/pubmed/2645138