Properties of mammalian nuclear-envelope nucleoside triphosphatase
The nucleoside triphosphatase activities of the nuclear envelopes from rat liver, pig liver and simian-virus-40-transformed mouse-embryo 3T3 cells were shown to exhibit similar parperties. All three preparations hydrolyse ATP, 2'-dATP, 3'-dATP, GTP, CTP and UTP in the presence of Mg2+, Ca2...
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| Veröffentlicht in: | Biochemical journal 1979-09, Vol.181 (3), p.647-658 |
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| creator | Agutter, P S Cockrill, J B Lavine, J E McCaldin, B Sim, R B |
| description | The nucleoside triphosphatase activities of the nuclear envelopes from rat liver, pig liver and simian-virus-40-transformed mouse-embryo 3T3 cells were shown to exhibit similar parperties. All three preparations hydrolyse ATP, 2'-dATP, 3'-dATP, GTP, CTP and UTP in the presence of Mg2+, Ca2+, Mn2+ and Co2+ with a pH optimum of 8.0, are sensitive to inhibition by mercurials, arsenicals, quercetin, proflavin and adenosine 5'-[gamma-thio]triphosphate and are partially inactivated by exposure to high ionic strength. The kinetic behaviour is similar for all substrates irrespective of the source of material. The typical Eadie-Hofstee plot, which is concave upwards at pH 8.0 when the ionic strength is 20mM, becomes linear when the pH is increased to 8.5 or the ionic strength to 160mM. The overall evidence, particularly the labelling of only one polypeptide by [gamma-32P]ATP, suggests that under the conditions of preparation and assay used only one class of nucleoside triphosphatase active sites is detectable in nuclear envelopes. The importance of these results for an understanding of the role of the enzyme in vivo is discussed. |
| doi_str_mv | 10.1042/bj1810647 |
| format | Article |
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All three preparations hydrolyse ATP, 2'-dATP, 3'-dATP, GTP, CTP and UTP in the presence of Mg2+, Ca2+, Mn2+ and Co2+ with a pH optimum of 8.0, are sensitive to inhibition by mercurials, arsenicals, quercetin, proflavin and adenosine 5'-[gamma-thio]triphosphate and are partially inactivated by exposure to high ionic strength. The kinetic behaviour is similar for all substrates irrespective of the source of material. The typical Eadie-Hofstee plot, which is concave upwards at pH 8.0 when the ionic strength is 20mM, becomes linear when the pH is increased to 8.5 or the ionic strength to 160mM. The overall evidence, particularly the labelling of only one polypeptide by [gamma-32P]ATP, suggests that under the conditions of preparation and assay used only one class of nucleoside triphosphatase active sites is detectable in nuclear envelopes. The importance of these results for an understanding of the role of the enzyme in vivo is discussed.</description><identifier>ISSN: 0264-6021</identifier><identifier>EISSN: 1470-8728</identifier><identifier>DOI: 10.1042/bj1810647</identifier><identifier>PMID: 229821</identifier><language>eng</language><publisher>England</publisher><subject>Adenine - analogs & derivatives ; Adenine - pharmacology ; Animals ; Cells, Cultured ; Kinetics ; Liver - enzymology ; Mice ; Nuclear Envelope - enzymology ; Nucleotides ; Osmolar Concentration ; Phosphoric Monoester Hydrolases - antagonists & inhibitors ; Phosphoric Monoester Hydrolases - metabolism ; Rats ; Substrate Specificity ; Sulfhydryl Reagents - pharmacology ; Swine</subject><ispartof>Biochemical journal, 1979-09, Vol.181 (3), p.647-658</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c369t-7b0fbcec73872033cc7573f35b95b3285b8ad95101eab85936108cbfd13d92fb3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1161204/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1161204/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/229821$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Agutter, P S</creatorcontrib><creatorcontrib>Cockrill, J B</creatorcontrib><creatorcontrib>Lavine, J E</creatorcontrib><creatorcontrib>McCaldin, B</creatorcontrib><creatorcontrib>Sim, R B</creatorcontrib><title>Properties of mammalian nuclear-envelope nucleoside triphosphatase</title><title>Biochemical journal</title><addtitle>Biochem J</addtitle><description>The nucleoside triphosphatase activities of the nuclear envelopes from rat liver, pig liver and simian-virus-40-transformed mouse-embryo 3T3 cells were shown to exhibit similar parperties. All three preparations hydrolyse ATP, 2'-dATP, 3'-dATP, GTP, CTP and UTP in the presence of Mg2+, Ca2+, Mn2+ and Co2+ with a pH optimum of 8.0, are sensitive to inhibition by mercurials, arsenicals, quercetin, proflavin and adenosine 5'-[gamma-thio]triphosphate and are partially inactivated by exposure to high ionic strength. The kinetic behaviour is similar for all substrates irrespective of the source of material. The typical Eadie-Hofstee plot, which is concave upwards at pH 8.0 when the ionic strength is 20mM, becomes linear when the pH is increased to 8.5 or the ionic strength to 160mM. The overall evidence, particularly the labelling of only one polypeptide by [gamma-32P]ATP, suggests that under the conditions of preparation and assay used only one class of nucleoside triphosphatase active sites is detectable in nuclear envelopes. The importance of these results for an understanding of the role of the enzyme in vivo is discussed.</description><subject>Adenine - analogs & derivatives</subject><subject>Adenine - pharmacology</subject><subject>Animals</subject><subject>Cells, Cultured</subject><subject>Kinetics</subject><subject>Liver - enzymology</subject><subject>Mice</subject><subject>Nuclear Envelope - enzymology</subject><subject>Nucleotides</subject><subject>Osmolar Concentration</subject><subject>Phosphoric Monoester Hydrolases - antagonists & inhibitors</subject><subject>Phosphoric Monoester Hydrolases - metabolism</subject><subject>Rats</subject><subject>Substrate Specificity</subject><subject>Sulfhydryl Reagents - pharmacology</subject><subject>Swine</subject><issn>0264-6021</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1979</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkEtLxDAURoP4GkcX7l10Jbio3jyatBtBB18woAtdhyRNnQxtU5N2wH9vpcOgqwv3Hr77cRA6x3CNgZEbvcY5Bs7EHpphJiDNBcn30QwIZykHgo_RSYxrAMyAwRE6JKTICZ6h-7fgOxt6Z2Piq6RRTaNqp9qkHUxtVUhtu7H1iEwLH11pkz64buVjt1K9ivYUHVSqjvZsO-fo4_HhffGcLl-fXhZ3y9RQXvSp0FBpY42gYzeg1BiRCVrRTBeZpiTPdK7KIsOArdJ5VlCOITe6KjEtC1JpOke3U2436MaWxrZ9ULXsgmtU-JZeOfn_0rqV_PQbiTHHBNgYcLkNCP5rsLGXjYvG1rVqrR-iFGxUwoGP4NUEmuBjDLbaPcEgf33Lne-RvfjbakdOgukP9KJ8lg</recordid><startdate>19790901</startdate><enddate>19790901</enddate><creator>Agutter, P S</creator><creator>Cockrill, J B</creator><creator>Lavine, J E</creator><creator>McCaldin, B</creator><creator>Sim, R B</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19790901</creationdate><title>Properties of mammalian nuclear-envelope nucleoside triphosphatase</title><author>Agutter, P S ; Cockrill, J B ; Lavine, J E ; McCaldin, B ; Sim, R B</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c369t-7b0fbcec73872033cc7573f35b95b3285b8ad95101eab85936108cbfd13d92fb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1979</creationdate><topic>Adenine - analogs & derivatives</topic><topic>Adenine - pharmacology</topic><topic>Animals</topic><topic>Cells, Cultured</topic><topic>Kinetics</topic><topic>Liver - enzymology</topic><topic>Mice</topic><topic>Nuclear Envelope - enzymology</topic><topic>Nucleotides</topic><topic>Osmolar Concentration</topic><topic>Phosphoric Monoester Hydrolases - antagonists & inhibitors</topic><topic>Phosphoric Monoester Hydrolases - metabolism</topic><topic>Rats</topic><topic>Substrate Specificity</topic><topic>Sulfhydryl Reagents - pharmacology</topic><topic>Swine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Agutter, P S</creatorcontrib><creatorcontrib>Cockrill, J B</creatorcontrib><creatorcontrib>Lavine, J E</creatorcontrib><creatorcontrib>McCaldin, B</creatorcontrib><creatorcontrib>Sim, R B</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biochemical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Agutter, P S</au><au>Cockrill, J B</au><au>Lavine, J E</au><au>McCaldin, B</au><au>Sim, R B</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Properties of mammalian nuclear-envelope nucleoside triphosphatase</atitle><jtitle>Biochemical journal</jtitle><addtitle>Biochem J</addtitle><date>1979-09-01</date><risdate>1979</risdate><volume>181</volume><issue>3</issue><spage>647</spage><epage>658</epage><pages>647-658</pages><issn>0264-6021</issn><eissn>1470-8728</eissn><abstract>The nucleoside triphosphatase activities of the nuclear envelopes from rat liver, pig liver and simian-virus-40-transformed mouse-embryo 3T3 cells were shown to exhibit similar parperties. All three preparations hydrolyse ATP, 2'-dATP, 3'-dATP, GTP, CTP and UTP in the presence of Mg2+, Ca2+, Mn2+ and Co2+ with a pH optimum of 8.0, are sensitive to inhibition by mercurials, arsenicals, quercetin, proflavin and adenosine 5'-[gamma-thio]triphosphate and are partially inactivated by exposure to high ionic strength. The kinetic behaviour is similar for all substrates irrespective of the source of material. The typical Eadie-Hofstee plot, which is concave upwards at pH 8.0 when the ionic strength is 20mM, becomes linear when the pH is increased to 8.5 or the ionic strength to 160mM. The overall evidence, particularly the labelling of only one polypeptide by [gamma-32P]ATP, suggests that under the conditions of preparation and assay used only one class of nucleoside triphosphatase active sites is detectable in nuclear envelopes. The importance of these results for an understanding of the role of the enzyme in vivo is discussed.</abstract><cop>England</cop><pmid>229821</pmid><doi>10.1042/bj1810647</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0264-6021 |
| ispartof | Biochemical journal, 1979-09, Vol.181 (3), p.647-658 |
| issn | 0264-6021 1470-8728 |
| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Adenine - analogs & derivatives Adenine - pharmacology Animals Cells, Cultured Kinetics Liver - enzymology Mice Nuclear Envelope - enzymology Nucleotides Osmolar Concentration Phosphoric Monoester Hydrolases - antagonists & inhibitors Phosphoric Monoester Hydrolases - metabolism Rats Substrate Specificity Sulfhydryl Reagents - pharmacology Swine |
| title | Properties of mammalian nuclear-envelope nucleoside triphosphatase |
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