Susceptibility of cord blood antioxidant enzymes glutathione reductase, glutathione peroxidase and glutathione S-transferase to different antibiotics: In vitro approach

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Cord blood has numerous facilities for life and used in many different areas. Cord blood contains many different catalytic proteins including antioxidant enzymes. Here we purified human cord blood glutathione reductase (hcbGR), glutathione S-transferase (hcbGST) and human cord blood glutathione peroxidase (hcbGPx) from human cord blood erythrocytes and analyzed the inhibition effects of the antibiotics incorporating cefuroxime, ceftriaxone, ceftizoxime and cefoperazone, on these enzymes. KI values for the drugs ranged from 10.42 to 28.72 M for hcbGR, 32.7 to 244.8 M for hcbGPx, and 32.39 to 267.3 M for hcbGST. Cefuroxime caused the highest inhibition on all enzymes with KI values of 10.42, 32.39, 32.7 M for hcbGR, hcbGST, and hcbGPx, respectively. All drugs displayed non-competitive inhibition regardless of their structures. Since these drugs are often used during pregnancy, identification of possible undesired impacts on various parameters has a great importance for pharmacological and medical applications. © 2013 Informa UK, Ltd.

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AlanDeğerDil
dc.contributor.authorEkinci, Deniz
dc.contributor.authorCankaya, Murat
dc.contributor.authorGül, Ilhami
dc.contributor.authorCoban, Taha Abdulkadir
dc.date.accessioned2026-10-18T20:30:33.063592108Z
dc.date.available2026-10-18T20:30:33.063592108Z
dc.date.issued2013
dc.description.abstractCord blood has numerous facilities for life and used in many different areas. Cord blood contains many different catalytic proteins including antioxidant enzymes. Here we purified human cord blood glutathione reductase (hcbGR), glutathione S-transferase (hcbGST) and human cord blood glutathione peroxidase (hcbGPx) from human cord blood erythrocytes and analyzed the inhibition effects of the antibiotics incorporating cefuroxime, ceftriaxone, ceftizoxime and cefoperazone, on these enzymes. KI values for the drugs ranged from 10.42 to 28.72 M for hcbGR, 32.7 to 244.8 M for hcbGPx, and 32.39 to 267.3 M for hcbGST. Cefuroxime caused the highest inhibition on all enzymes with KI values of 10.42, 32.39, 32.7 M for hcbGR, hcbGST, and hcbGPx, respectively. All drugs displayed non-competitive inhibition regardless of their structures. Since these drugs are often used during pregnancy, identification of possible undesired impacts on various parameters has a great importance for pharmacological and medical applications. © 2013 Informa UK, Ltd.
dc.identifier.doi10.3109/14756366.2012.688042
dc.identifier.eissn1475-6374
dc.identifier.endpage829
dc.identifier.issn1475-6374
dc.identifier.issue4
dc.identifier.pmid22630073
dc.identifier.scopus2-s2.0-84880062864
dc.identifier.startpage824
dc.identifier.urihttps://rdlopen.rawdatalibrary.net/r/ebyu/15702
dc.identifier.volume28
dc.identifier.wosWOS:000321693400023
dc.language.isoen
dc.publisherTAYLOR & FRANCIS LTD
dc.relation.ispartofJournal of Enzyme Inhibition and Medicinal Chemistry
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectAntibiotic
dc.subjectCord blood
dc.subjectGlutathione
dc.subjectInhibition
dc.subjectAnti-Bacterial Agents
dc.subjectAntioxidants
dc.subjectCefoperazone
dc.subjectCeftizoxime
dc.subjectCeftriaxone
dc.subjectCefuroxime
dc.subjectDose-Response Relationship, Drug
dc.subjectErythrocytes
dc.subjectGlutathione Peroxidase
dc.subjectGlutathione Reductase
dc.subjectGlutathione Transferase
dc.subjectHumans
dc.subjectMolecular Structure
dc.subjectStructure-Activity Relationship
dc.subjectantibiotic agent
dc.subjectantibiotic sensitivity
dc.subjectarticle
dc.subjectcontrolled study
dc.subjectenzyme activity
dc.subjectenzyme inhibition
dc.subjecterythrocyte
dc.subjectfemale
dc.subjecthuman
dc.subjecthuman cell
dc.subjectin vitro study
dc.subjectpregnancy
dc.titleSusceptibility of cord blood antioxidant enzymes glutathione reductase, glutathione peroxidase and glutathione S-transferase to different antibiotics: In vitro approach
dc.typeArticle
dspace.entity.typePublication
rdl.citation.scopus8
rdl.citation.wos7
rdl.oa.statusgreen
rdl.source.indexSCOPUS
rdl.source.indexWOS
rdl.wos.indexScience Citation Index Expanded (SCI-EXPANDED)