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dc.contributor.authorFontecha, F. Javier-
dc.contributor.authorRequena, Teresa-
dc.contributor.authorSwaisgood, H. E-
dc.date.accessioned2015-05-28T07:42:26Z-
dc.date.available2015-05-28T07:42:26Z-
dc.date.issued1996-
dc.identifierdoi: 10.1111/j.1472-765X.1996.tb01181-
dc.identifierissn: 0266-8254-
dc.identifier.citationLetters in Applied Microbiology 22: 371- 374 (1996)-
dc.identifier.urihttp://hdl.handle.net/10261/115826-
dc.description.abstractThis study describes an affinity chromatography procedure for proteinase purification using bioselective binding to immobilized bacitracin. By coupling bacitracin to controlled-pore glass (CPG) beads, an affinity matrix was obtained that permitted rapid purification of proteinases under conditions that minimize autolysis. Bacitracin-CPG was used to bioselectively adsorb the extracellular proteinase secreted by Enterococcus faecalis var. liquefaciens IFPL 383. The overall purification obtained with this procedure was 5149-fold. The ability of bacitracin-CPG to bind other proteinases was examined using various commercial proteinases. The specific activities of subtilin BPN' and proteinase K were increased by bioselective adsorption and excellent recoveries of all proteinases applied were obtained.-
dc.description.sponsorshipThis work was carried out under the terms of reference of research projects ALI94-0735, FEOGA 11 16/92, ESP 4-IV and AAIR 2-CT93-1531.-
dc.publisherBlackwell Publishing-
dc.rightsclosedAccess-
dc.titleAffinity chromatography of proteinases using bacitracin immobilized to porous glass beads-
dc.typeArtículo-
dc.identifier.doi10.1111/j.1472-765X.1996.tb01181-
dc.date.updated2015-05-28T07:42:26Z-
dc.description.versionPeer Reviewed-
dc.language.rfc3066eng-
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