Purification and properties of glucose 6-phosphate dehydrogenase from coriander (Coriandrum sativum) leaves
Özet
Glucose-6-phosphate dehydrogenase (D-glucose-6-phosphate: NADP(+) oxidoreductase, EC 1.1.1.49; G6PD) was purified from coriander (Coriandrum sativum) leaves; the kinetic behavior and some properties of the enzyme were also investigated. The purification was done at 4C and involved two steps: ammonium sulfate fractionation, and DEAF-Sephadex A50 ion exchange chromatography. The enzyme was obtained with a yield of 26.4% and had a specific activity of 1.826 U/mg protein. Optimum pH, stable pH, optimum temperature, molecular weight, K-M and V-max values for NADP(+) and glucose 6-phosphate (G6-P) were also determined.
Atıf için künye
DEMIR, H., BEYDEMIR, O., CIFTCI, M., & Küfrevioğlu, Ö. İ. (2004). Purification and properties of glucose 6-phosphate dehydrogenase from coriander (Coriandrum sativum) leaves. JOURNAL OF FOOD BIOCHEMISTRY, 28(2), 155–168. https://doi.org/10.1111/j.1745-4514.2004.tb00062.x
BibTeX
@article{demir2004-68780,
author = {DEMIR, H and BEYDEMIR, O and CIFTCI, M and Küfrevioğlu, Ömer İrfan},
title = {Purification and properties of glucose 6-phosphate dehydrogenase from coriander (Coriandrum sativum) leaves},
journal = {JOURNAL OF FOOD BIOCHEMISTRY},
year = {2004},
volume = {28},
number = {2},
pages = {155--168},
issn = {0145-8884},
doi = {10.1111/j.1745-4514.2004.tb00062.x},
url = {https://akademik.atauni.edu.tr/yayinlar/68780-purification-and-properties-of-glucose-6-phosphate-dehydrogenase-from-coriander}
}