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Journals / Hacettepe Journal of Biology and Chemistry / 2012 / Cilt: 40 - Sayı: 2

Purification and Characterization of α-Carbonic Anhydrase II from Sheep Liver and Examining the Inhibition Effect of Kanamycin on Enzyme Activity

Koyun Karaciğerinden a-Karbonik Anhidraz II’ nin Saflaştırılması ve Karakterizasyonu ve Enzim Aktivitesi Üzerine Kanamisinin İnhibisyon Etkisinin İncelenmesi

Veysel ÇOMAKLI
Emrah YERLİKAYA
Ramazan DEMİRDAĞ
Ömer İrfan KÜFREVİOĞLU
Pages
133–138
Publication Date
2012-04-01
DOI
—
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AI Summary & Key Takeaways

AI Insight
⚡ TL;DR(Too Long; Didn't Read)

Kanamycin ex- hibited in vitro inhibitory effect on the enzyme activity.

📌 3 Key Takeaways

🎯
Objective & Hypothesis:Sheep carbonic anhydrase - II SCA-II E.C: 4.2.1.1 was purified from sheep liver and some characteristic properties were investigated.
📊
Key Findings & Data:The enzyme was purified approximate 43.1-fold with a yield of 38.6%, and a specific activity of 4000 EU/mg proteins.
💡
Conclusion & Impact:Kanamycin ex- hibited in vitro inhibitory effect on the enzyme activity.
🔬Design:Research Article
📍Scope:Comprehensive Sample
⚙️Variables:Karakterizasyon · Karbonik Anhidraz · Koyun

Abstract

Sheep carbonic anhydrase - II SCA-II E.C: 4.2.1.1 was purified from sheep liver and some characteristic properties were investigated. The enzyme was purified approximate 43.1-fold with a yield of 38.6%, and a specific activity of 4000 EU/mg proteins. For the enzyme, optimum pH, optimum temperature, optimum ionic strength and stable pH were determined to be 7.5, 40ºC, 10 mM and 8.5, respectively. The molecular weight was found 29 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis SDS-PAGE . Kanamycin ex- hibited in vitro inhibitory effect on the enzyme activity.

Özet

K oyun karbonik anhidraz-II E.C: 4.2.1.1 enzimi koyun karaciğerinden saflaştırıldı ve bazı karakteristik özellikleri araştırıldı. Enzim 4000 EU/mg protein spesifik aktivitesi ve % 38.6 verim ile yaklaşık olarak 43,1 kat saflaştırıldı. Enzim için optimum pH, optimum sıcaklık, optimum iyonik şiddet ve stabil pH sırasıyla 7.5, 40ºC, 10 mM ve 8.5 olarak belirlendi. Moleküler ağırlığı sodyum dodesil sülfat poliakrilamid jel elektroforezi ile 29 kDa olarak bulundu. Kanamisinin enzim aktivitesi üzerine in vitro inhibitör etkisi incelendi

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Cite This Article

ÇOMAKLI, V., YERLİKAYA, E., DEMİRDAĞ, R., KÜFREVİOĞLU, Ö. İ. (2012). Purification and Characterization of α-Carbonic Anhydrase II from Sheep Liver and Examining the Inhibition Effect of Kanamycin on Enzyme Activity. Hacettepe Journal of Biology and Chemistry, Cilt: 40 - Sayı: 2, 133–138. https://ajindex.com/articles/256248

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References (2)

  1. C.T. Supuran, Carbonic anhydrases: novel therapeutic applications for inhibitors and activators, Drug Discov. Nature Rev., 7 (2008) 81. C.T. Supuran, A. Scozzafava, A. Casini, Carbonic anhydrase inhibitors, Med. Res. Rev., 23 (2003) 146. C.T. Supuran, Carbonic anhydrases—an overview, Curr.Pharm. Des., 14 (2008) 603. C.T. Supuran, Carbonic anhydrase inhibition with natural products: novel chemotypes and inhibition mechanisms, Mol. Divers., 15 (2011) 305. J.B. Feldstein, D.N Silvarman, Purufication and characterization of carbonic anhydrase from the saliva of the rat, J. Biol. Chem., 259(1984) 5447. S.R. Krungkrai, N. Suraveratum, S. Rochanakij and J. Krungkrai, Characterization of carbonic anhydrase in Plasmodium falciparum, Int. J. Parasit., 31 (2001) 661. S. Beydemir, I. Gülcin, Effect of melatonin on carbonic anhydrase from human erythrocyte in vitro and from rat erythrocyte in vivo, J. Enzyme Inhib. Medic. Chem., 19 (2004) 193. M. Hilvo, M. Tolvanen, A. Clark, B. Shen, GN. Shah, A. Waheed, P. Hamli, M. Hänninen, J.M. Hämäläinen, M. Vihinen, WS. Sly, S. Parkkila, Characterization of CA XV, a new GPI-anchored form of carbonic anhydrase, Biochem. J., 392 (2005) 83. C.T. Supuran, Carbonic anhydrases: catalytic and inhibition mechanisms, distribution and physiological roles, In carbonic anhydrase. ıts inhibitors and activators (Supuran C.T et al., eds), CRC Press. (2004) 1. K.M. Wilbur, N.G. Anderson, Electrometric and colorometric determination of carbonic anhydrase, J Biol Chem. 176 (1976) 147. J.A. Verpoorte, S. Mehta, J.T. Edsall, Esterase activities of human carbonic anhydrases, B. and C.J. Biol. Chem., 242 (1967) 4221. M.M. Bradford, A rapid and sensitive method for the quantition of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem., 72 (1976) 248. D.K. Laemmli, Cleavage of structural proteins during assembly of the head of bacteriophage T4, Nature, 227 (1970) 680. http://www.drugs.com /mtm / kanamycin.html 25.07.2011
  2. H. Lineweaver, D. Burk, The determination of enzyme dissocation constants, J. Am. Chem. Soc., 57 (1934) 685. E. Bayram, M. Senturk, O.I Kufrevioglu, C.T. Supuran, In vitro inhibition of salicylic acid derivatives on human cytosolic carbonic anhydrase isozymes I and II, Bioorg. Med. Chem., 16 (2008) 9101. M. Senturk, I. Gulcin, A. Dastan, O.I. Kufrevioglu, C.T. Supuran, Carbonic anhydrase inhibitors: Inhibitor of human erythrocyte I and II isoenzymes with antioxidant phenolic compounds, Bioorg.M