In vitro effects of some purine analogues on human carbonic anhydrase CA, EC 4.2.1.1 were investigated in this study. Human erythrocyte CA-I and CA-II isozymes were purified using Sepharose-4B-aniline-sulfanilamide affinity gel chromatography. Specific activity and yields were determined as 904.08 EU mg-1, 59.86%; 6469.23 EU mg-1, 56.82%, respectively. The overall purification was approximately 105.74-fold for hCA-I and 756.64- fold for hCA-II. The inhibitory effects of different nucleoside analogues on CA activity were determined at low concentrations using the esterase method under in vitro conditions. I50 values for diprophylline, acyclovir, proxyphylline, aminophylline and caffeine were calculated from activity % -[I] as 4.12 μM, 5.58 μM, 9.96 μM, 19.17 mM, and 23.21 mM for hCA-I and 1.19 μM, 2.57 μM, 4.29 μM, 4.71 mM and 4.94 mM for hCA-II respectively. Additonally, the Lineweaver-Burk curves obtained were used for the determination of Ki and the inhibitor type for diprophylline, acyclovir and poxyphylline. Abbreviations: CA, carbonic anhydrase; hCA-I, human carbonic anhydrase I; hCA-II, human carbonic anhydrase II.
Carbonic anhydrase Nucleoside analogue Inhibition hCA-I hCA-II
Birincil Dil | İngilizce |
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Bölüm | Research Article |
Yazarlar | |
Yayımlanma Tarihi | 1 Aralık 2009 |
Yayımlandığı Sayı | Yıl 2009 Cilt: 37 Sayı: 4 |
HACETTEPE JOURNAL OF BIOLOGY AND CHEMİSTRY
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