A highly active alkaline phosphatase from the marine bacterium cobetia
An alkaline phosphatase with unusually high specific activity has been found to be produced by the marine bacterium Cobetia marina (strain KMM MC-296) isolated from coelomic liquid of the mussel Crenomytilus grayanus. The properties of enzyme, such as a very high specific activity (15000 DE U/1 mg o...
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| Veröffentlicht in: | Marine biotechnology (New York, N.Y.) N.Y.), 2005-05, Vol.7 (3), p.173-178 |
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| container_title | Marine biotechnology (New York, N.Y.) |
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| creator | Yu Plisova, E Balabanova, L A Ivanova, E P Kozhemyako, V B Mikhailov, V V Agafonova, E V Rasskazov, V A |
| description | An alkaline phosphatase with unusually high specific activity has been found to be produced by the marine bacterium Cobetia marina (strain KMM MC-296) isolated from coelomic liquid of the mussel Crenomytilus grayanus. The properties of enzyme, such as a very high specific activity (15000 DE U/1 mg of protein), no activation with divalent cations, resistance to high concentrations of inorganic phosphorus, as well as substrate specificity toward 5' nucleotides suggest that the enzyme falls in an intermediate position between unspecific alkaline phosphatases (EC 3.1.3.1) and 5' nucleotidases (EC 3.1.3.5). |
| doi_str_mv | 10.1007/s10126-004-3022-4 |
| format | Article |
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The properties of enzyme, such as a very high specific activity (15000 DE U/1 mg of protein), no activation with divalent cations, resistance to high concentrations of inorganic phosphorus, as well as substrate specificity toward 5' nucleotides suggest that the enzyme falls in an intermediate position between unspecific alkaline phosphatases (EC 3.1.3.1) and 5' nucleotidases (EC 3.1.3.5).</description><identifier>ISSN: 1436-2228</identifier><identifier>EISSN: 1436-2236</identifier><identifier>DOI: 10.1007/s10126-004-3022-4</identifier><identifier>PMID: 15906116</identifier><language>eng</language><publisher>United States: Springer Nature B.V</publisher><subject>5'-Nucleotidase - isolation & purification ; Alkaline Phosphatase - isolation & purification ; Animals ; Cations ; Enzymes ; Halomonadaceae - enzymology ; Hydrogen-Ion Concentration ; Isoelectric Point ; Microbiology ; Molecular Weight ; Mytilidae - microbiology ; Pacific Ocean ; Phosphatase ; Substrate Specificity</subject><ispartof>Marine biotechnology (New York, N.Y.), 2005-05, Vol.7 (3), p.173-178</ispartof><rights>Springer Science+Business Media, Inc. 2005</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c421t-a832a57bf0ccc33e277af74dc32086ae574fe603d22086c94a30858d2d9835383</citedby><cites>FETCH-LOGICAL-c421t-a832a57bf0ccc33e277af74dc32086ae574fe603d22086c94a30858d2d9835383</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15906116$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yu Plisova, E</creatorcontrib><creatorcontrib>Balabanova, L A</creatorcontrib><creatorcontrib>Ivanova, E P</creatorcontrib><creatorcontrib>Kozhemyako, V B</creatorcontrib><creatorcontrib>Mikhailov, V V</creatorcontrib><creatorcontrib>Agafonova, E V</creatorcontrib><creatorcontrib>Rasskazov, V A</creatorcontrib><title>A highly active alkaline phosphatase from the marine bacterium cobetia</title><title>Marine biotechnology (New York, N.Y.)</title><addtitle>Mar Biotechnol (NY)</addtitle><description>An alkaline phosphatase with unusually high specific activity has been found to be produced by the marine bacterium Cobetia marina (strain KMM MC-296) isolated from coelomic liquid of the mussel Crenomytilus grayanus. 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The properties of enzyme, such as a very high specific activity (15000 DE U/1 mg of protein), no activation with divalent cations, resistance to high concentrations of inorganic phosphorus, as well as substrate specificity toward 5' nucleotides suggest that the enzyme falls in an intermediate position between unspecific alkaline phosphatases (EC 3.1.3.1) and 5' nucleotidases (EC 3.1.3.5).</abstract><cop>United States</cop><pub>Springer Nature B.V</pub><pmid>15906116</pmid><doi>10.1007/s10126-004-3022-4</doi><tpages>6</tpages></addata></record> |
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| identifier | ISSN: 1436-2228 |
| ispartof | Marine biotechnology (New York, N.Y.), 2005-05, Vol.7 (3), p.173-178 |
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| language | eng |
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| source | MEDLINE; SpringerLink Journals - AutoHoldings |
| subjects | 5'-Nucleotidase - isolation & purification Alkaline Phosphatase - isolation & purification Animals Cations Enzymes Halomonadaceae - enzymology Hydrogen-Ion Concentration Isoelectric Point Microbiology Molecular Weight Mytilidae - microbiology Pacific Ocean Phosphatase Substrate Specificity |
| title | A highly active alkaline phosphatase from the marine bacterium cobetia |
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