Phosphatases and phosphodiesterases isolated from the red king crab (Paralithodes camtschatica) hepatopancreas
Five enzymes have been isolated from the hepatopancreas of the red king crab Paralithodes camtschatica by means of ion exchange and gel chromatography: two acid (AcP) and one alkaline (AlkP) phosphomonoesterases, one alkaline phosphodiesterase (AlkPI), and one acid phosphodiesterase (AcPD). The pH o...
Gespeichert in:
Veröffentlicht in: | Applied biochemistry and microbiology 2008-01, Vol.44 (1), p.93-97 |
---|---|
Hauptverfasser: | , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 97 |
---|---|
container_issue | 1 |
container_start_page | 93 |
container_title | Applied biochemistry and microbiology |
container_volume | 44 |
creator | Menzorova, N I Ivleva, A D Sibirtsev, Yu T Rasskazov, V A |
description | Five enzymes have been isolated from the hepatopancreas of the red king crab Paralithodes camtschatica by means of ion exchange and gel chromatography: two acid (AcP) and one alkaline (AlkP) phosphomonoesterases, one alkaline phosphodiesterase (AlkPI), and one acid phosphodiesterase (AcPD). The pH optimum values of these enzymes are: AlkPs and AlkPD, 7.5; AcP, 5.5; and AcPD, 5.0. The activity of AlkP and AlkPD demands Mg2+ ions. The molecular weights of the enzymes (kDa) are the following: AlkP, 80; AcPs, 80 and 82; AlkPD, 51; and AcPD, 57. The enzymes are relatively thermostable (ID 50 from 47 to 62°C). AlkP is inhibited by NaCl (IC 50 at 0.4 M). The AcP, AcPD, and AlkPD activities are tolerant of high ionic strength. [PUBLICATION ABSTRACT] |
doi_str_mv | 10.1007/s10438-008-1016-0 |
format | Article |
fullrecord | <record><control><sourceid>proquest</sourceid><recordid>TN_cdi_proquest_miscellaneous_20656613</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>20656613</sourcerecordid><originalsourceid>FETCH-LOGICAL-p128t-97101208d8f86d21d4c926305f5f19a14382b7b57828cc6ed73e670a114f9f5b3</originalsourceid><addsrcrecordid>eNpdkM1OwzAQhC0EEqXwANwsDggOgbWd2M4RVfxJlegBztXGsUlKGgfbeX-swonTakazo_2WkEsGdwxA3UcGpdAFgC4YMFnAEVkwmZUAXh6TBQCIQmqhT8lZjLssa6nrBRk3nY9ThwmjjRTHlk4Hw7e9jcmGg91HP2CyLXXB72nqLA1ZfPXjJzUBG3qzwYBDn_JWThvcp2hyZW_wlnZ2wuQnHE2wGM_JicMh2ou_uSQfT4_vq5di_fb8unpYFxPjOhW1yhAcdKudli1nbWlqLgVUrnKsRpZReaOaSmmujZG2VcJKBchY6WpXNWJJrn97p-C_50yy3ffR2GHA0fo5bjnISkomcvDqX3Dn5zDm27Zc5M_WTJXiB6dZaX0</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>231009174</pqid></control><display><type>article</type><title>Phosphatases and phosphodiesterases isolated from the red king crab (Paralithodes camtschatica) hepatopancreas</title><source>SpringerLink Journals - AutoHoldings</source><creator>Menzorova, N I ; Ivleva, A D ; Sibirtsev, Yu T ; Rasskazov, V A</creator><creatorcontrib>Menzorova, N I ; Ivleva, A D ; Sibirtsev, Yu T ; Rasskazov, V A</creatorcontrib><description>Five enzymes have been isolated from the hepatopancreas of the red king crab Paralithodes camtschatica by means of ion exchange and gel chromatography: two acid (AcP) and one alkaline (AlkP) phosphomonoesterases, one alkaline phosphodiesterase (AlkPI), and one acid phosphodiesterase (AcPD). The pH optimum values of these enzymes are: AlkPs and AlkPD, 7.5; AcP, 5.5; and AcPD, 5.0. The activity of AlkP and AlkPD demands Mg2+ ions. The molecular weights of the enzymes (kDa) are the following: AlkP, 80; AcPs, 80 and 82; AlkPD, 51; and AcPD, 57. The enzymes are relatively thermostable (ID 50 from 47 to 62°C). AlkP is inhibited by NaCl (IC 50 at 0.4 M). The AcP, AcPD, and AlkPD activities are tolerant of high ionic strength. [PUBLICATION ABSTRACT]</description><identifier>ISSN: 0003-6838</identifier><identifier>EISSN: 1608-3024</identifier><identifier>DOI: 10.1007/s10438-008-1016-0</identifier><language>eng</language><publisher>Dordrecht: Springer Nature B.V</publisher><subject>Chromatography ; Crustaceans ; Decapoda ; Enzymes ; Marine ; Marine biology ; Paralithodes camtschatica ; Sodium chloride</subject><ispartof>Applied biochemistry and microbiology, 2008-01, Vol.44 (1), p.93-97</ispartof><rights>2008</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids></links><search><creatorcontrib>Menzorova, N I</creatorcontrib><creatorcontrib>Ivleva, A D</creatorcontrib><creatorcontrib>Sibirtsev, Yu T</creatorcontrib><creatorcontrib>Rasskazov, V A</creatorcontrib><title>Phosphatases and phosphodiesterases isolated from the red king crab (Paralithodes camtschatica) hepatopancreas</title><title>Applied biochemistry and microbiology</title><description>Five enzymes have been isolated from the hepatopancreas of the red king crab Paralithodes camtschatica by means of ion exchange and gel chromatography: two acid (AcP) and one alkaline (AlkP) phosphomonoesterases, one alkaline phosphodiesterase (AlkPI), and one acid phosphodiesterase (AcPD). The pH optimum values of these enzymes are: AlkPs and AlkPD, 7.5; AcP, 5.5; and AcPD, 5.0. The activity of AlkP and AlkPD demands Mg2+ ions. The molecular weights of the enzymes (kDa) are the following: AlkP, 80; AcPs, 80 and 82; AlkPD, 51; and AcPD, 57. The enzymes are relatively thermostable (ID 50 from 47 to 62°C). AlkP is inhibited by NaCl (IC 50 at 0.4 M). The AcP, AcPD, and AlkPD activities are tolerant of high ionic strength. [PUBLICATION ABSTRACT]</description><subject>Chromatography</subject><subject>Crustaceans</subject><subject>Decapoda</subject><subject>Enzymes</subject><subject>Marine</subject><subject>Marine biology</subject><subject>Paralithodes camtschatica</subject><subject>Sodium chloride</subject><issn>0003-6838</issn><issn>1608-3024</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNpdkM1OwzAQhC0EEqXwANwsDggOgbWd2M4RVfxJlegBztXGsUlKGgfbeX-swonTakazo_2WkEsGdwxA3UcGpdAFgC4YMFnAEVkwmZUAXh6TBQCIQmqhT8lZjLssa6nrBRk3nY9ThwmjjRTHlk4Hw7e9jcmGg91HP2CyLXXB72nqLA1ZfPXjJzUBG3qzwYBDn_JWThvcp2hyZW_wlnZ2wuQnHE2wGM_JicMh2ou_uSQfT4_vq5di_fb8unpYFxPjOhW1yhAcdKudli1nbWlqLgVUrnKsRpZReaOaSmmujZG2VcJKBchY6WpXNWJJrn97p-C_50yy3ffR2GHA0fo5bjnISkomcvDqX3Dn5zDm27Zc5M_WTJXiB6dZaX0</recordid><startdate>20080101</startdate><enddate>20080101</enddate><creator>Menzorova, N I</creator><creator>Ivleva, A D</creator><creator>Sibirtsev, Yu T</creator><creator>Rasskazov, V A</creator><general>Springer Nature B.V</general><scope>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>F1W</scope><scope>H95</scope><scope>H99</scope><scope>L.F</scope><scope>L.G</scope></search><sort><creationdate>20080101</creationdate><title>Phosphatases and phosphodiesterases isolated from the red king crab (Paralithodes camtschatica) hepatopancreas</title><author>Menzorova, N I ; Ivleva, A D ; Sibirtsev, Yu T ; Rasskazov, V A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p128t-97101208d8f86d21d4c926305f5f19a14382b7b57828cc6ed73e670a114f9f5b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Chromatography</topic><topic>Crustaceans</topic><topic>Decapoda</topic><topic>Enzymes</topic><topic>Marine</topic><topic>Marine biology</topic><topic>Paralithodes camtschatica</topic><topic>Sodium chloride</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Menzorova, N I</creatorcontrib><creatorcontrib>Ivleva, A D</creatorcontrib><creatorcontrib>Sibirtsev, Yu T</creatorcontrib><creatorcontrib>Rasskazov, V A</creatorcontrib><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>ASFA: Marine Biotechnology Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Marine Biotechnology Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><jtitle>Applied biochemistry and microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Menzorova, N I</au><au>Ivleva, A D</au><au>Sibirtsev, Yu T</au><au>Rasskazov, V A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phosphatases and phosphodiesterases isolated from the red king crab (Paralithodes camtschatica) hepatopancreas</atitle><jtitle>Applied biochemistry and microbiology</jtitle><date>2008-01-01</date><risdate>2008</risdate><volume>44</volume><issue>1</issue><spage>93</spage><epage>97</epage><pages>93-97</pages><issn>0003-6838</issn><eissn>1608-3024</eissn><abstract>Five enzymes have been isolated from the hepatopancreas of the red king crab Paralithodes camtschatica by means of ion exchange and gel chromatography: two acid (AcP) and one alkaline (AlkP) phosphomonoesterases, one alkaline phosphodiesterase (AlkPI), and one acid phosphodiesterase (AcPD). The pH optimum values of these enzymes are: AlkPs and AlkPD, 7.5; AcP, 5.5; and AcPD, 5.0. The activity of AlkP and AlkPD demands Mg2+ ions. The molecular weights of the enzymes (kDa) are the following: AlkP, 80; AcPs, 80 and 82; AlkPD, 51; and AcPD, 57. The enzymes are relatively thermostable (ID 50 from 47 to 62°C). AlkP is inhibited by NaCl (IC 50 at 0.4 M). The AcP, AcPD, and AlkPD activities are tolerant of high ionic strength. [PUBLICATION ABSTRACT]</abstract><cop>Dordrecht</cop><pub>Springer Nature B.V</pub><doi>10.1007/s10438-008-1016-0</doi><tpages>5</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0003-6838 |
ispartof | Applied biochemistry and microbiology, 2008-01, Vol.44 (1), p.93-97 |
issn | 0003-6838 1608-3024 |
language | eng |
recordid | cdi_proquest_miscellaneous_20656613 |
source | SpringerLink Journals - AutoHoldings |
subjects | Chromatography Crustaceans Decapoda Enzymes Marine Marine biology Paralithodes camtschatica Sodium chloride |
title | Phosphatases and phosphodiesterases isolated from the red king crab (Paralithodes camtschatica) hepatopancreas |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-27T03%3A13%3A32IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Phosphatases%20and%20phosphodiesterases%20isolated%20from%20the%20red%20king%20crab%20(Paralithodes%20camtschatica)%20hepatopancreas&rft.jtitle=Applied%20biochemistry%20and%20microbiology&rft.au=Menzorova,%20N%20I&rft.date=2008-01-01&rft.volume=44&rft.issue=1&rft.spage=93&rft.epage=97&rft.pages=93-97&rft.issn=0003-6838&rft.eissn=1608-3024&rft_id=info:doi/10.1007/s10438-008-1016-0&rft_dat=%3Cproquest%3E20656613%3C/proquest%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=231009174&rft_id=info:pmid/&rfr_iscdi=true |