Yazarlar (5) |
![]() Ağrı İbrahim Çeçen Üniversitesi, Türkiye |
![]() Ağrı İbrahim Çeçen Üniversitesi, Türkiye |
![]() Ağrı İbrahim Çeçen Üniversitesi, Türkiye |
![]() Siirt Üniversitesi, Türkiye |
![]() Ağrı İbrahim Çeçen Üniversitesi, Türkiye |
Özet |
Carbonic anhydrase (CA) was purified from Ağrı Balık Lake trout gill (fCA) by affinity chromatography on a sepharose 4B-tyrosine-sulfanilamide column. The fCA enzyme was purified with about a 303.9 purification factor, a specific activity 4130.4 EU (mg-protein)(-1), and a yield of 79.3 by using sepharose-4B-L tyrosine-sulfanilamide affinity gel chromatography. The molecular weight determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was found to be about 29.9 kDa. The kinetic parameters, K(M) and V(max) were determined for the 4-nitrophenyl acetate hydrolysis reaction. Some sulfonamides were tested as inhibitors against the purified CA enzymes. The Ki constants for mafenide (1), p-toluenesulfonamide (2), 2-bromo-benzene sulfonamide (3), 4-chlorobenzene sulfonamide (4), 4-amino-6-chloro-1-3 benzenedisulfonamide (5), sulfamethazine (6), sulfaguanidine (7), sulfadiazine (8), and acetozazolamide (9) were in the range of 7.5-108.75 μM. |
Anahtar Kelimeler |
Ağrı Balık Lake Trout | Carbonic Anhydrase | Characterization | Inhibition | Purification | Sulfonamides |
Makale Türü | Özgün Makale |
Makale Alt Türü | SSCI, AHCI, SCI, SCI-Exp dergilerinde yayımlanan tam makale |
Dergi Adı | JOURNAL OF BIOCHEMICAL AND MOLECULAR TOXICOLOGY |
Dergi ISSN | 1095-6670 Wos Dergi Scopus Dergi |
Dergi Tarandığı Indeksler | SCI-Expanded |
Makale Dili | İngilizce |
Basım Tarihi | 03-2015 |
Cilt No | 29 |
Sayı | 3 |
Sayfalar | 123 / 128 |
Doi Numarası | 10.1002/jbt.21675 |
Makale Linki | http://doi.wiley.com/10.1002/jbt.21675 |