Phosphatase activity of Poa pratensis seeds. II. Purification and characterization of acid phosphatase Ia2 and Ia3
Two acid phosphatases (Ia2, Ia3) have been isolated from Poa pratensis seeds and partially purified. Both enzymes showed maximal activity at pH 4,9. They exhibited high activity towards p-nitrophenyl phosphate, inorganic pyrophosphate and phenyl phosphate, much less activity towards glucose-6 phosph...
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| Format: | Article |
| Language: | English |
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Polish Botanical Society
2015-01-01
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| Series: | Acta Societatis Botanicorum Poloniae |
| Online Access: | https://pbsociety.org.pl/journals/index.php/asbp/article/view/5021 |
| _version_ | 1818913052166193152 |
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| author | I. Lorenc-Kubis B. Morawiecka M. Niezgódka A. Hebrowska |
| author_facet | I. Lorenc-Kubis B. Morawiecka M. Niezgódka A. Hebrowska |
| author_sort | I. Lorenc-Kubis |
| collection | DOAJ |
| description | Two acid phosphatases (Ia2, Ia3) have been isolated from Poa pratensis seeds and partially purified. Both enzymes showed maximal activity at pH 4,9. They exhibited high activity towards p-nitrophenyl phosphate, inorganic pyrophosphate and phenyl phosphate, much less activity towards glucose-6 phosphate, and mononucleotides. Phosphatases a2 and a3 differed in their activity towards ADP. Orthophosphate, fluoride and Zn2+ were effective inhibitors. EDTA, β-mercaptoethanol and Mg2+ activated phophatase a2 but had no effect on phosphatase a3. Zn2+ inhibited the activity of phosphatase a2 noncompetitively, whereas phosphatase a3 showed inhibition of mixed type. Trypsin, chymotrypsin and pronase had no effect on the enzyme activities of both molecular forms. |
| first_indexed | 2024-12-19T23:24:21Z |
| format | Article |
| id | doaj.art-294c1f680e04408fa45ef6fa00261106 |
| institution | Directory Open Access Journal |
| issn | 2083-9480 |
| language | English |
| last_indexed | 2024-12-19T23:24:21Z |
| publishDate | 2015-01-01 |
| publisher | Polish Botanical Society |
| record_format | Article |
| series | Acta Societatis Botanicorum Poloniae |
| spelling | doaj.art-294c1f680e04408fa45ef6fa002611062022-12-21T20:01:54ZengPolish Botanical SocietyActa Societatis Botanicorum Poloniae2083-94802015-01-0144225526310.5586/asbp.1975.0224223Phosphatase activity of Poa pratensis seeds. II. Purification and characterization of acid phosphatase Ia2 and Ia3I. Lorenc-Kubis0B. Morawiecka1M. Niezgódka2A. Hebrowska3University of WrocławUniversity of WrocławUniversity of WrocławUniversity of WrocławTwo acid phosphatases (Ia2, Ia3) have been isolated from Poa pratensis seeds and partially purified. Both enzymes showed maximal activity at pH 4,9. They exhibited high activity towards p-nitrophenyl phosphate, inorganic pyrophosphate and phenyl phosphate, much less activity towards glucose-6 phosphate, and mononucleotides. Phosphatases a2 and a3 differed in their activity towards ADP. Orthophosphate, fluoride and Zn2+ were effective inhibitors. EDTA, β-mercaptoethanol and Mg2+ activated phophatase a2 but had no effect on phosphatase a3. Zn2+ inhibited the activity of phosphatase a2 noncompetitively, whereas phosphatase a3 showed inhibition of mixed type. Trypsin, chymotrypsin and pronase had no effect on the enzyme activities of both molecular forms.https://pbsociety.org.pl/journals/index.php/asbp/article/view/5021 |
| spellingShingle | I. Lorenc-Kubis B. Morawiecka M. Niezgódka A. Hebrowska Phosphatase activity of Poa pratensis seeds. II. Purification and characterization of acid phosphatase Ia2 and Ia3 Acta Societatis Botanicorum Poloniae |
| title | Phosphatase activity of Poa pratensis seeds. II. Purification and characterization of acid phosphatase Ia2 and Ia3 |
| title_full | Phosphatase activity of Poa pratensis seeds. II. Purification and characterization of acid phosphatase Ia2 and Ia3 |
| title_fullStr | Phosphatase activity of Poa pratensis seeds. II. Purification and characterization of acid phosphatase Ia2 and Ia3 |
| title_full_unstemmed | Phosphatase activity of Poa pratensis seeds. II. Purification and characterization of acid phosphatase Ia2 and Ia3 |
| title_short | Phosphatase activity of Poa pratensis seeds. II. Purification and characterization of acid phosphatase Ia2 and Ia3 |
| title_sort | phosphatase activity of poa pratensis seeds ii purification and characterization of acid phosphatase ia2 and ia3 |
| url | https://pbsociety.org.pl/journals/index.php/asbp/article/view/5021 |
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