Purification and characterization of glucose 6-phosphate dehydrogenase from sheep erythrocytes and inhibitory effects of some antibiotics on enzyme activity
Özet
Glucose 6-phosphate dehydrogenase (D-glucose 6-phosphate: NADP(+) oxidoreductase, EC 1.1.1.49; G6PD) was purified from sheep erythrocytes, using a simple and rapid method. The purification consisted of three steps; preparation of haemolysate, ammonium sulphate fractionation and 2', 5'-ADP Sepharose 4B affinity chromatography. The enzyme was obtained with a yield of 37.1% and had a specific activity of 4.64 U/mg proteins. Optimal pH, stable pH, molecular weight, and K-M and V-max values for NADP(+) and glucose 6-phosphate (G6-P) substrates were also determined for the enzyme.
Anahtar kelimeler
Atıf için künye
Beydemir, S., Ciftci, M., & Küfrevioğlu, Ö. İ. (2002). Purification and characterization of glucose 6-phosphate dehydrogenase from sheep erythrocytes and inhibitory effects of some antibiotics on enzyme activity. JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, 17(4), 271–277. https://doi.org/10.1080/1475636021000010941
BibTeX
@article{beydemir2002-68759,
author = {Beydemir, S and Ciftci, M and Küfrevioğlu, Ömer İrfan},
title = {Purification and characterization of glucose 6-phosphate dehydrogenase from sheep erythrocytes and inhibitory effects of some antibiotics on enzyme activity},
journal = {JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY},
year = {2002},
volume = {17},
number = {4},
pages = {271--277},
issn = {1475-6366},
doi = {10.1080/1475636021000010941},
url = {https://akademik.atauni.edu.tr/yayinlar/68759-purification-and-characterization-of-glucose-6-phosphate-dehydrogenase-from}
}