Title of article
Purification and enzymatic characterization of alkaline phosphatase from Pinctada fucata
Author/Authors
Xiao، نويسنده , , Rui and Xie، نويسنده , , Li-Ping and Lin، نويسنده , , Jing-Yu and Li، نويسنده , , Chong-Hua and Chen، نويسنده , , Qing-Xi and Zhou، نويسنده , , Hai-Meng and Zhang، نويسنده , , Rong-Qing، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 2002
Pages
10
From page
65
To page
74
Abstract
An alkaline phosphatase was purified from Pinctada fucata, a kind of pearl oyster, by chromatography on DEAE-32 cellulose, Sephadex G-150 and DEAE A-25. The specific activity of the enzyme was 2040 U mg−1. The kinetics characteristics of the enzyme have been studied. The product HPO42− and the product-analog WO43− competitively inhibited the enzyme activity. Positive monovalent cations had no effect on the enzyme activity, while positive bivalent cations had different effects on the enzyme: Mg2+, Ca2+, Co2+ and Mn2+ activated the enzyme while Zn2+, Cu2+ and Cd2+ inhibited the enzyme.
Keywords
Purification , alkaline phosphatase , Mollusc , Kinetics , Pinctada fucata
Journal title
Journal of Molecular Catalysis B Enzymatic
Serial Year
2002
Journal title
Journal of Molecular Catalysis B Enzymatic
Record number
1715945
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