Evaluation of Inhibition Effects of Some Cardiovascular Therapeutics on Human Erythrocyte Carbonic Anhydrase Isoenzymes

MakaleYalnız künye

Özet

Carbonic anhydrase enzyme plays a vital role in metabolic events such as acid-base regulation and respiration. Inour research, it is tried to determine the inhibitory influences of the cardiovascular therapeutics esmololhydrochloride, amiodarone hydrochloride and lidocaine hydrochloride on human erythrocytes carbonic anhydrases(hCA I and II). In accordance with this purpose, carbonic anhydrase isoenzymes were purified from humanerythrocytes by using affinity chromatography method. Enzyme purity was checked by SDS-PAGEelectrophoresis method. After the carbonic anhydrase enzymes were purified, the inhibitory affects ofcardiovascular therapeutics on these enzymes, using esterase activity, which is the method of measuring in vitroactivity, were examined. The three cardiovascular therapeutics dose-dependently decreased activity of hCAs. IC50values of amiodarone hydrochloride, esmolol hydrochloride and lidocaine hydrochloride were found to be,respectively, 0.91 mM, 5 mM, 5.8 mM for hCA-I and 0.41 mM, 3.5 mM, and 6.36 mM for hCA-II. Our resultsproved that, under in vitro conditions, cardiovascular therapeutics significantly inhibit human CA-I and IIactivities. So, irregular use of these medicines may cause serious adverse effects in terms of human health.

Anahtar Kelimeler

RDL Kalıcı Bağlantı (PID)
https://rdlopen.rawdatalibrary.net/r/bayburt/15288Resmi atıflarda kullanılan kalıcı adres
İndeks kayıtları
Kaydın indeks veri tabanlarındaki sayfası (aktarımda alınan kayıt numarasıyla). Erişim, indeksin kendi koşullarına bağlıdır.
Atıflar
TR Dizin
2
Her kaynağın kendi saydığı toplam atıf; aktarım ve zenginleştirme sırasında alındı.
Tam Kayıt
AlanDeğerDil
dc.contributor.authorIsgor, Mehmet Mustafa
dc.contributor.authorKılınç, Namık
dc.contributor.authorAlim, Zuhal
dc.contributor.authorBeydemir, Şükrü
dc.contributor.authorSengül, Bülent
dc.date.accessioned2026-10-29T19:20:18.194454686Z
dc.date.available2026-10-29T19:20:18.194454686Z
dc.date.issued2018
dc.description.abstractCarbonic anhydrase enzyme plays a vital role in metabolic events such as acid-base regulation and respiration. Inour research, it is tried to determine the inhibitory influences of the cardiovascular therapeutics esmololhydrochloride, amiodarone hydrochloride and lidocaine hydrochloride on human erythrocytes carbonic anhydrases(hCA I and II). In accordance with this purpose, carbonic anhydrase isoenzymes were purified from humanerythrocytes by using affinity chromatography method. Enzyme purity was checked by SDS-PAGEelectrophoresis method. After the carbonic anhydrase enzymes were purified, the inhibitory affects ofcardiovascular therapeutics on these enzymes, using esterase activity, which is the method of measuring in vitroactivity, were examined. The three cardiovascular therapeutics dose-dependently decreased activity of hCAs. IC50values of amiodarone hydrochloride, esmolol hydrochloride and lidocaine hydrochloride were found to be,respectively, 0.91 mM, 5 mM, 5.8 mM for hCA-I and 0.41 mM, 3.5 mM, and 6.36 mM for hCA-II. Our resultsproved that, under in vitro conditions, cardiovascular therapeutics significantly inhibit human CA-I and IIactivities. So, irregular use of these medicines may cause serious adverse effects in terms of human health.
dc.identifier.eissn2147-3188
dc.identifier.endpage97
dc.identifier.issn2147-3129
dc.identifier.issue1
dc.identifier.startpage90
dc.identifier.urihttps://rdlopen.rawdatalibrary.net/r/bayburt/15288
dc.identifier.volume7
dc.language.isoen
dc.relation.ispartofBitlis Eren Üniversitesi Fen Bilimleri Dergisi
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectTıbbi Araştırmalar Deneysel
dc.subjectGenel ve Dahili Tıp
dc.subjectKimya, Tıbbi
dc.subjectBiyokimya ve Moleküler Biyoloji
dc.subjectKalp ve Kalp Damar Sistemi
dc.subjectFarmakoloji ve Eczacılık
dc.titleEvaluation of Inhibition Effects of Some Cardiovascular Therapeutics on Human Erythrocyte Carbonic Anhydrase Isoenzymes
dc.typeArticle
rdl.citation.trdizin2
rdl.source.indexTRDIZIN