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- W2368555513 abstract "A 5′-nucleotidase was isolated and purified from the snake venom of T. albolabris using three steps of chromatography including DEAE-SephadexA-25, Sephadex-G-100 and CM-Sephadex C-50. Using SDS-PAGE and HPLC column chromatography the purified 5′-nucleotidase proved to be homogenous. It was a glycoprotein with a molecular weight of 48.03 kDa. The enzymatic activities of the purified 5′-nucleotidase were 330.33 μg Pi/min mg and 123.56 μg Pi/min mg when using AMP(adenosine monophosphate) and ADP(adenosine diphosphate) as substrates, respectively. Metal ions, including Zn2+, Fe3+ and Cu2+, could inhibit 5′-nucleotidase activity, as did EDTA. Its optimum pH was nine and its optimum temperature was 50°C. It has a potent inhibitory effect on rabbit platelet aggregation induced by ADP." @default.
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- W2368555513 date "2008-01-01" @default.
- W2368555513 modified "2023-09-24" @default.
- W2368555513 title "Purification and Characterization of 5′-nucleotidase from Trimeresurus albolabris Venom" @default.
- W2368555513 hasPublicationYear "2008" @default.
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