• Türkçe
    • English
  • English 
    • Türkçe
    • English
  • Login
View Item 
  •   RTEÜ
  • Araştırma Çıktıları | TR-Dizin | WoS | Scopus | PubMed
  • WoS İndeksli Yayınlar Koleksiyonu
  • View Item
  •   RTEÜ
  • Araştırma Çıktıları | TR-Dizin | WoS | Scopus | PubMed
  • WoS İndeksli Yayınlar Koleksiyonu
  • View Item
JavaScript is disabled for your browser. Some features of this site may not work without it.

Characterization and inhibition studies of carbonic anhydrase from gill of Russian Sturgeon Fish (Acipenser gueldenstaedtii)

View/Open

Tam Metin / Full Text (545.2Kb)

Access

info:eu-repo/semantics/closedAccess

Date

2016

Author

Dincer, Barbaros
Ekinci, Arife Pınar
Akyüz, Gülay
Kurtoğlu, İlker Zeki

Metadata

Show full item record

Citation

Dinçer, B., Ekinci, A. P., Akyüz, G., & Kurtoğlu, İ. Z. (2016). Characterization and inhibition studies of carbonic anhydrase from gill of Russian Sturgeon Fish (Acipenser gueldenstaedtii). Journal of enzyme inhibition and medicinal chemistry, 31(6), 1662–1665. https://doi.org/10.3109/14756366.2015.1076810

Abstract

An alpha-carbonic anhydrase (CA, EC 4.2.1.1) was purified and characterized kinetically from gill of Acipenser gueldenstaedtii as an endangered sturgeon species. the carbonic anhydrase was purified 66-folds with yield 20.7% by Sepharose-4B-L-tyrosine-sulfanilamide affinity column and the specific activity was determined as 222.2 EU/mg protein. K-m and V-max kinetic values for gill carbonic anhydrase were calculated by a Lineweaver-Burk graph using p-nitrophenol acetate (p-NPA) as a substrate, and was defined as 2.5mM and 5 x 10(6) mu M/min, respectively. It was observed that CA from the sturgeon gill in the presence of the sulfanilamide and acetazolamide as an inhibitor had very low IC50 values such as 13.0 and 0.1 mu M, respectively. in addition, it was determined that the enzyme was inhibited by Fe-2+,Fe- Co-2+,Co- Ni2+, and Zn2+-Ba2+ with the IC50 values of 0.2, 1.7, 1.2, and 1.1 mM, respectively.

Source

Journal of Enzyme Inhibition and Medicinal Chemistry

Volume

31

Issue

6

URI

https://doi.org/10.3109/14756366.2015.1076810
https://hdl.handle.net/11436/2654

Collections

  • FEF, Kimya Bölümü Koleksiyonu [476]
  • PubMed İndeksli Yayınlar Koleksiyonu [2443]
  • Scopus İndeksli Yayınlar Koleksiyonu [5990]
  • SUF, Su Ürünleri Yetiştiriciliği Bölümü Koleksiyonu [162]
  • WoS İndeksli Yayınlar Koleksiyonu [5260]



DSpace software copyright © 2002-2015  DuraSpace
Contact Us | Send Feedback
Theme by 
@mire NV
 

 




| Instruction | Guide | Contact |

DSpace@RTEÜ

by OpenAIRE
Advanced Search

sherpa/romeo

Browse

All of DSpaceCommunities & CollectionsBy Issue DateAuthorsTitlesSubjectsTypeLanguageDepartmentCategoryPublisherAccess TypeInstitution AuthorThis CollectionBy Issue DateAuthorsTitlesSubjectsTypeLanguageDepartmentCategoryPublisherAccess TypeInstitution Author

My Account

LoginRegister

Statistics

View Google Analytics Statistics

DSpace software copyright © 2002-2015  DuraSpace
Contact Us | Send Feedback
Theme by 
@mire NV
 

 


|| Guide|| Instruction || Library || Recep Tayyip Erdoğan University || OAI-PMH ||

Recep Tayyip Erdoğan University, Rize, Turkey
If you find any errors in content, please contact:

Creative Commons License
Recep Tayyip Erdoğan University Institutional Repository is licensed under a Creative Commons Attribution-NonCommercial-NoDerivs 4.0 Unported License..

DSpace@RTEÜ:


DSpace 6.2

tarafından İdeal DSpace hizmetleri çerçevesinde özelleştirilerek kurulmuştur.