The Phosphomonoesterase Activity ofBasidiomycetes Agaricus Campestris
| Autor: | L. Vandendriessche, L. Dehennin, J. Stockx |
|---|---|
| Rok vydání: | 1961 |
| Předmět: |
chemistry.chemical_classification
Agaricus campestris biology Physiology Agaricus Basidiomycota Fungi Acid phosphatase Phosphate biology.organism_classification Biochemistry Phosphoric Monoester Hydrolases Boric acid Dephosphorylation chemistry.chemical_compound Enzyme chemistry biology.protein Urea Thermal stability |
| Zdroj: | Archives Internationales de Physiologie et de Biochimie. 69:79-88 |
| ISSN: | 0003-9799 |
| DOI: | 10.3109/13813456109092780 |
| Popis: | It has been shown that Basidiomyceles Agaricus campestris contains an acid phosphatase with pH optimum 5.5. It dephosphorylates monophenyl phosphate, 1- and 2-glycerophosphate and the (2′ + 3′)-ribonucleotides. Marked differences have been found in the dephosphorylation rates of these different substrates. Maximal thermal stability is found around pH 5.5. The enzymic activity is only weakly influenced by variations in ionic strength.It is inhibited by NaF, (COONa)2′ Cu++, Na2HAsO4, Na2MoO4, and D-tartrate. Boric acid exerts a slight inhibitory effect and Mg++, EDTA and cystein do not interfere with its activity. Activity is more or less destroyed by H2O2, urea and ethanol.According to the characteristics of the enzyme it is to be listed as belonging to type II of the classification of Roche (1950). |
| Databáze: | OpenAIRE |
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