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Inhibitory properties of some heavy metals on carbonic anhydrase I and II isozymes activities purified from Van Lake fish (Chalcalburnus Tarichi) gill       
Yazarlar (5)
Prof. Dr. Müslüm KUZU Prof. Dr. Müslüm KUZU
Ağrı İbrahim Çeçen Üniversitesi, Türkiye
Veysal Çomaklı
Ağrı İbrahim Çeçen Üniversitesi, Türkiye
Ebru Akkemik
Siirt Üniversitesi, Türkiye
Mehmet Çiftci
Bingöl Üniversitesi, Türkiye
Ömer İrfan Küfrevioğlu
Atatürk Üniversitesi, Türkiye
Devamını Göster
Özet
In this study, CA I and II isoenzymes were purified from Van Lake fish gills by using Sepharose-4B-L-tyrosine-sulfanilamide affinity chromatography and to determine the effects of some metals on the enzyme activities. For purified CA I isoenzyme, yield, specific activity, and purification fold were obtained as 42.07%, 4948.12 EU/mg protein, and 116.61 and for CA II isoenzyme, 7%, 1798.56 EU/mg protein, and 42.38 respectively. Activity of CA was determined by measuring "CO-hydratase activity". Purity control was checked by SDS-PAGE. In vitro inhibitory effect of Cu, Ag, Cd, Ni metal ions, and arsenic (V) oxide were also examined for both isozymes activities. Whereas Cu, Ag, Cd, and Ni ions showed inhibitory effects on both isozymes, arsenic (V) oxide showed activation effect. IC values were calculated by drawing activity %-[I] graphs for metal ions exhibiting inhibitory effects. IC values were determined as 3.39, 6.38, 13.52, and 206 μM for CA I isozyme and 6.16, 20.29, 46, and 223 μM for CA II isozyme respectively.
Anahtar Kelimeler
Carbonic anhydrase | Heavy metal | Inhibition | Purification
Makale Türü Özgün Makale
Makale Alt Türü SSCI, AHCI, SCI, SCI-Exp dergilerinde yayımlanan tam makale
Dergi Adı FISH PHYSIOLOGY AND BIOCHEMISTRY
Dergi ISSN 0920-1742 Wos Dergi Scopus Dergi
Dergi Tarandığı Indeksler SCI-Expanded
Makale Dili İngilizce
Basım Tarihi 08-2018
Cilt No 44
Sayı 4
Sayfalar 1119 / 1125
Doi Numarası 10.1007/s10695-018-0499-8
Makale Linki http://link.springer.com/10.1007/s10695-018-0499-8