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Purification and characterization of 6-PGD from quail liver

By Salih Hamzah

Purification and characterization of 6-PGD from quail liver

0 - Default Title
Description
In this study, 6-phosphogluconate dehydrogenase (6PGD) enzyme was purified from the quail liver by using ammonium sulphate precipitation, and 2', 5'-ADP Sepharose 4B affinity chromatography methods, with specific activities 14.6 EU/mg, 89% yield and 112 purification fold. Enzyme activity was measured spectrophotometrically at 340 nm. SDS-PAGE checked the purity of the enzyme. The molecular weight of purified enzyme by the SDS-PAGE method was calculated to be 44 KDa. Protein determination was performed by the Bradford method. For the enzyme optimal pH (8.0), stable pH (8.0), optimum ionic strength (600 mM in Tris-HCl) optimal temperature (60°C) were determined. In addition KM and Vmax values for 6-phosphogluconate (6-PGA) and NADP+ were calculated as 0.058 and 0.0015 mM; 0.0078 and 0.057 EU/ml respectively.
Product details
Binding:
Paperback
Number of Pages:
56
Release Date:
2025-11-03
Publication Date:
2025-11-03
Publisher:
LAP LAMBERT Academic Publishing
Languages:
Original: English
ISBN10:
6209172849
ISBN13:
9786209172847
Weight:
102 g
Height:
150 cm
Width:
220 cm
Thickness:
4 cm
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