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Purification and properties of glucose 6-phosphate dehydrogenase from turkey erythrocytes
NOPR - NISCAIR Online Periodicals Repository
View Archive Info| Field | Value | |
| Title |
Purification and properties of glucose 6-phosphate dehydrogenase from turkey erythrocytes
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| Creator |
Yılmaz, Hayrullah
Beydemir, Sukru Bakan, Ebubekir Kufrevioglu, O Irfan |
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| Description |
62-65
Glucose 6-phosphate dehydrogenase (G6PD) was purified from turkey erythrocytes by ammonium sulphate precipitation and followed by ADP Sepharose affinity gel chromatography. The yield was 49.71% and specific activity of the enzyme was found to be 44.16 EU/mg protein. By gel filtration the molecular mass was found to be 75 kDa. The enzyme had an optimum pH at 9.0, and optimum temperature at 50oC. Km and Vmax for NADP+ and glucose 6- phosphate (G6-P) as substrates were also determined and effects of inhibitors such as ATP, NADH and NADPH were examined. |
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| Date |
2009-04-06T09:27:30Z
2009-04-06T09:27:30Z 2003-02 |
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| Type |
Article
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| Identifier |
0301-1208
http://hdl.handle.net/123456789/3742 |
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| Language |
en_US
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| Publisher |
CSIR
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| Source |
IJBB Vol.40(1) [February 2003]
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