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KMID : 0364219820250020071
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Korean Journal of Zoology
1982 Volume.25 No. 2 p.71 ~ p.80
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Studies on the Alkaline Phosphatase of Pekin Duck: I. Some Properties of Liver Alkaline Phosphatase
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Kang Shin-Sung
Park Tae-Kyu
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Abstract
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Some properties of alkaline phosphatase, partially purified from the liver of the local Pekin duck, Anas platyrhynchos, were investigated with the following results. 1. Gel-filtration of the duck liver extract indicated the presence of two molecular-weight species of alkaline phosphatase. 2. Electrophoresis of both enzyme preparations suggests the presence of two molecular forms of alkaline phosphatase with different physicochemical characteristics. 3. The liver alkaline phosphatase has an optimum pH of 9.0, and is further activated by $Mg^2+$ but not by $Ca^2+$. 4. The enzyme was relatively heat-labile, and was competitively inhibited by phosphate ions, but uncompetitively inhibited by L-phenylalanine. 5. These results are discussed in comparison with the properties of human and other animal alkaline phosphatases.
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