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dc.contributor.authorBaran, ET
dc.contributor.authorOzer, N
dc.contributor.authorHasirci, V
dc.date.accessioned2019-12-16T10:29:38Z
dc.date.available2019-12-16T10:29:38Z
dc.date.issued2003
dc.identifier.issn1570-0232
dc.identifier.urihttps://doi.org/10.1016/S1570-0232(03)00487-2
dc.identifier.urihttp://hdl.handle.net/11655/20151
dc.description.abstractIn the present study antileukemic enzyme L-asparaginase (ASNase) and catalase (as a model enzyme) were modified in solid-phase with activated polyethylene glycol (PEG,) by using ligand-immobilized affinity column systems L-asparagine-Sepharose CL-4B and Procion red-Sepharose CL-4B, respectively. Studies on change of specific activity with modification time showed negligible differences between batches of modified catalase. Modification of ASNase for I It resulted in 50.2% recovery of the specific activity and the attachment of 69 molecules of PEG(2) per molecule of ASNase forming 'PEGylated ASNase'. Sequential modification of ASNase by activated PEG and heparin resulted in coupling of about nine molecules of heparin per molecule of PEGylated ASNase. Intravenous (i.v.) administration of PEG(2)-modified ASNase showed prolonged presence in the blood circulation and no adverse effects or symptoms of anaphylaxis were observed in presensitized mice. (C) 2003 Elsevier B.V. All rights reserved.
dc.language.isoen
dc.publisherElsevier Science Bv
dc.relation.isversionof10.1016/S1570-0232(03)00487-2
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectBiochemistry & Molecular Biology
dc.subjectChemistry
dc.titleSolid-Phase Enzyme Modification Via Affinity Chromatography
dc.typeinfo:eu-repo/semantics/article
dc.relation.journalJournal Of Chromatography B-Analytical Technologies In The Biomedical And Life Sciences
dc.contributor.departmentBiyokimya
dc.identifier.volume794
dc.identifier.issue2
dc.identifier.startpage311
dc.identifier.endpage322
dc.description.indexWoS


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