Effects of some drugs on human cord blood erythrocyte carbonic anhydrases I and II: An in vitro study

ArticleAçık Erişim

Özet

In the present study, we purified hcbCA I and II from human cord blood erythrocytes using by Sepharose-4B-l tyrosine-sulfanilamide affinity gel chromatography. Also, it was checked the inhibition effects of ampicillin sulfate, ceftriaxone, ceftizoxime and ranitidine on hcbCA I and hcbCA II. IC50 values for ceftriaxone, ceftizoxime and ranitidine were found to be 27.l, 79.4 and 55.5 M for hcbCA I and of 21.0, 79.1 and 66.1 M for hcbCA II, respectively. According to these results, Ampicillin sulfate inhibited only hcbCAII and IC50 values of this antibiotic was found to be 56.8 M. All these substances were found non-competitive inhibitors. It is important to study the inhibition effects of these drugs on hcbCA I and II izoenzymes. Because, pregnant woman is take all of these substance. For this reason, these drugs should be carefully used and the dosage should be very well ordered to minimize side effects. © 2012 Informa UK, Ltd.

Anahtar Kelimeler

RDL Kalıcı Bağlantı (PID)
https://rdlopen.rawdatalibrary.net/r/ebyu/15784Resmi atıflarda kullanılan kalıcı adres
Tam Kayıt
AlanDeğerDil
dc.contributor.authorCankaya, Murat
dc.contributor.authorAktas, Mehmet
dc.contributor.authorKuzucu, Mehmet
dc.contributor.authorGül, Ilhami
dc.contributor.authorCoban, T. Abdulkadir
dc.date.accessioned2026-10-18T20:30:38.121274793Z
dc.date.available2026-10-18T20:30:38.121274793Z
dc.date.issued2012
dc.description.abstractIn the present study, we purified hcbCA I and II from human cord blood erythrocytes using by Sepharose-4B-l tyrosine-sulfanilamide affinity gel chromatography. Also, it was checked the inhibition effects of ampicillin sulfate, ceftriaxone, ceftizoxime and ranitidine on hcbCA I and hcbCA II. IC50 values for ceftriaxone, ceftizoxime and ranitidine were found to be 27.l, 79.4 and 55.5 M for hcbCA I and of 21.0, 79.1 and 66.1 M for hcbCA II, respectively. According to these results, Ampicillin sulfate inhibited only hcbCAII and IC50 values of this antibiotic was found to be 56.8 M. All these substances were found non-competitive inhibitors. It is important to study the inhibition effects of these drugs on hcbCA I and II izoenzymes. Because, pregnant woman is take all of these substance. For this reason, these drugs should be carefully used and the dosage should be very well ordered to minimize side effects. © 2012 Informa UK, Ltd.
dc.identifier.doi10.3109/14756366.2011.604852
dc.identifier.eissn1475-6374
dc.identifier.endpage645
dc.identifier.issn1475-6374
dc.identifier.issue5
dc.identifier.pmid21851212
dc.identifier.scopus2-s2.0-84866057425
dc.identifier.startpage641
dc.identifier.urihttps://rdlopen.rawdatalibrary.net/r/ebyu/15784
dc.identifier.volume27
dc.identifier.wosWOS:000308533100003
dc.language.isoen
dc.publisherTAYLOR & FRANCIS LTD
dc.relation.ispartofJournal of Enzyme Inhibition and Medicinal Chemistry
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectCarbonic anhydrase
dc.subjectCord blood
dc.subjectErythrocytes
dc.subjectCarbonic Anhydrase I
dc.subjectCarbonic Anhydrase II
dc.subjectCarbonic Anhydrase Inhibitors
dc.subjectChromatography, Affinity
dc.subjectElectrophoresis, Polyacrylamide Gel
dc.subjectFetal Blood
dc.subjectHumans
dc.subjectampicillin
dc.subjectampicillin sulfate
dc.subjectantibiotic agent
dc.subjectcarbonate dehydratase I
dc.subjectcarbonate dehydratase II
dc.subjectceftizoxime
dc.subjectranitidine
dc.subjectsepharose
dc.subjectsulfanilamide
dc.subjecttyrosine
dc.subjectunclassified drug
dc.subjectaffinity chromatography
dc.subjectaffinity gel chromatography
dc.subjectarticle
dc.subjectcontrolled study
dc.subjectdrug inhibition
dc.subjectdrug structure
dc.subjectenzyme activity
dc.subjectenzyme assay
dc.subjecterythrocyte
dc.titleEffects of some drugs on human cord blood erythrocyte carbonic anhydrases I and II: An in vitro study
dc.typeArticle
dspace.entity.typePublication
rdl.citation.scopus7
rdl.citation.wos9
rdl.departmentErzincan University, Science and Art Faculty, Biology Department, Erzincan, Turkey.
rdl.oa.statusgreen
rdl.source.indexSCOPUS
rdl.source.indexWOS
rdl.source.indexPUBMED
rdl.wos.indexScience Citation Index Expanded (SCI-EXPANDED)