Properties of an alkaline phosphatase from the dinoflagellate Peridinium cinctum |
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Institution: | 1. Institute of Biochemistry, Faculty of Veterinary Medicine, University of Bologna, Italy;2. Kinneret Limnological Laboratory, P.O. Box 345, Tiberias 14102, Israel;1. Physics Dept, University of Puerto Rico Mayagüez, 00681 USA;2. University of Zululand, KwaDlangezwa, 3886 South Africa |
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Abstract: | - 1.1. Alkaline phosphatase (EC 3.1.3.1) from the dinoflagellate Peridinium cinctum, the Lake Kinneret bloom alga, has been partially purified by gel filtration.
- 2.2. The enzyme could be easily extracted using a distilled water/chloroform mixture suggesting that the alkaline phosphatase of Peridinium is particularly labile.
- 3.3. The molecular weight of the enzyme was estimated as 158,000 ± 5000. The enzyme showed a broad pH optimum (in the range pH 8.0–8.5), had a Km of 0.45 mM for p-nitrophenylphosphate as substrate and was stable to repeated freeze/thawing cycles.
- 4.4. The enzyme was strongly activated by Mg2+ whereas Zn2+ (and to a lesser extent Cd2+) was an effective inhibitor of the enzyme. Cu2+ activated the enzyme at low concentrations, although at higher concentrations inhibited the enzyme. This effect of metals on the Peridinium alkaline phosphatase could be environmentally important since underwater hot springs, containing high concentrations of copper, enter the lake.
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