Localization of oxidized nocotinamide--adenine dinucleotide glycohydrolase in the mouse liver nuclear envelope
NAD+ glycohydrolase activity located in the nuclear envelope was maximally solubilized by treatment with 0.1--0.2% Triton X-100. The residual activity largely represents the chromatin-associated NAD+ glycohydrolase. Under these conditions the phospholipids were extensively solubilized (over 90%) whi...
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Veröffentlicht in: | Biochemical journal 1979-02, Vol.178 (2), p.467-473 |
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description | NAD+ glycohydrolase activity located in the nuclear envelope was maximally solubilized by treatment with 0.1--0.2% Triton X-100. The residual activity largely represents the chromatin-associated NAD+ glycohydrolase. Under these conditions the phospholipids were extensively solubilized (over 90%) while leaving the nuclei physically stable, although the nuclear membranes were removed, as shown by electron microscopy. After Triton X-100 treatment, deoxyribonuclease I did not significantly affect the residual NAD+ glycohydrolase activity, although the DNA was completely broken down. This enzyme activity can be released from the nuclear pellet by incubation with phospholipase C. For comparative studies, the glucose 6-phosphatase activity, known to be present in the nuclear envelope, was investigated. Treatment with 0.01% Triton X-100 released 10--20% of the phospholipids, but without solubilizing either glucose 6-phosphatase or NAD+ glycohydrolase. Higher Triton X-100 concentrations (0.1--1.0%) inhibited glucose 6-phosphatase, but not NAD+ glycohydrolase activity. NAD+ glycohydrolase is apparently present in a latent form in the nuclear envelope. Glucose 6-phosphatase, However, shows no such latency. |
doi_str_mv | 10.1042/bj1780467 |
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The residual activity largely represents the chromatin-associated NAD+ glycohydrolase. Under these conditions the phospholipids were extensively solubilized (over 90%) while leaving the nuclei physically stable, although the nuclear membranes were removed, as shown by electron microscopy. After Triton X-100 treatment, deoxyribonuclease I did not significantly affect the residual NAD+ glycohydrolase activity, although the DNA was completely broken down. This enzyme activity can be released from the nuclear pellet by incubation with phospholipase C. For comparative studies, the glucose 6-phosphatase activity, known to be present in the nuclear envelope, was investigated. Treatment with 0.01% Triton X-100 released 10--20% of the phospholipids, but without solubilizing either glucose 6-phosphatase or NAD+ glycohydrolase. Higher Triton X-100 concentrations (0.1--1.0%) inhibited glucose 6-phosphatase, but not NAD+ glycohydrolase activity. NAD+ glycohydrolase is apparently present in a latent form in the nuclear envelope. Glucose 6-phosphatase, However, shows no such latency.</description><identifier>ISSN: 0264-6021</identifier><identifier>ISSN: 0306-3283</identifier><identifier>EISSN: 1470-8728</identifier><identifier>DOI: 10.1042/bj1780467</identifier><identifier>PMID: 220967</identifier><language>eng</language><publisher>England</publisher><subject>Animals ; Chromatin - enzymology ; Deoxyribonucleases - pharmacology ; Glucose-6-Phosphatase - metabolism ; In Vitro Techniques ; Liver - enzymology ; Liver - ultrastructure ; Male ; Mice ; Microscopy, Electron ; NAD+ Nucleosidase - metabolism ; Nuclear Envelope - drug effects ; Nuclear Envelope - enzymology ; Nuclear Envelope - ultrastructure ; Phospholipases - pharmacology ; Phospholipids - metabolism ; Polyethylene Glycols - pharmacology</subject><ispartof>Biochemical journal, 1979-02, Vol.178 (2), p.467-473</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c2847-9c4625468c636c88865003e97337c05c14c454bf35920d53b3539304e0b5d2df3</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/PMC1186536/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1186536/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,724,777,781,882,27905,27906,53772,53774</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/220967$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tamulevicius, P</creatorcontrib><creatorcontrib>Streffer, C</creatorcontrib><creatorcontrib>Roscic, O</creatorcontrib><creatorcontrib>Hubert, E</creatorcontrib><title>Localization of oxidized nocotinamide--adenine dinucleotide glycohydrolase in the mouse liver nuclear envelope</title><title>Biochemical journal</title><addtitle>Biochem J</addtitle><description>NAD+ glycohydrolase activity located in the nuclear envelope was maximally solubilized by treatment with 0.1--0.2% Triton X-100. The residual activity largely represents the chromatin-associated NAD+ glycohydrolase. Under these conditions the phospholipids were extensively solubilized (over 90%) while leaving the nuclei physically stable, although the nuclear membranes were removed, as shown by electron microscopy. After Triton X-100 treatment, deoxyribonuclease I did not significantly affect the residual NAD+ glycohydrolase activity, although the DNA was completely broken down. This enzyme activity can be released from the nuclear pellet by incubation with phospholipase C. For comparative studies, the glucose 6-phosphatase activity, known to be present in the nuclear envelope, was investigated. Treatment with 0.01% Triton X-100 released 10--20% of the phospholipids, but without solubilizing either glucose 6-phosphatase or NAD+ glycohydrolase. Higher Triton X-100 concentrations (0.1--1.0%) inhibited glucose 6-phosphatase, but not NAD+ glycohydrolase activity. NAD+ glycohydrolase is apparently present in a latent form in the nuclear envelope. Glucose 6-phosphatase, However, shows no such latency.</description><subject>Animals</subject><subject>Chromatin - enzymology</subject><subject>Deoxyribonucleases - pharmacology</subject><subject>Glucose-6-Phosphatase - metabolism</subject><subject>In Vitro Techniques</subject><subject>Liver - enzymology</subject><subject>Liver - ultrastructure</subject><subject>Male</subject><subject>Mice</subject><subject>Microscopy, Electron</subject><subject>NAD+ Nucleosidase - metabolism</subject><subject>Nuclear Envelope - drug effects</subject><subject>Nuclear Envelope - enzymology</subject><subject>Nuclear Envelope - ultrastructure</subject><subject>Phospholipases - pharmacology</subject><subject>Phospholipids - metabolism</subject><subject>Polyethylene Glycols - pharmacology</subject><issn>0264-6021</issn><issn>0306-3283</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1979</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkb1vFDEQxS1EgEugoKdwhUSxMP7ebZBQFALSSWmgtrz2bM6R1z68eycuf32WXHQK1Wj0fnpvRo-Q9ww-M5D8S3_HTAtSmxdkxaSBpjW8fUlWwLVsNHD2hpxP0x0AkyDhNXnFOXTarEheF-9SvHdzLJmWgZa_McR7DDQXX-aY3RgDNo0LmGNGGmLe-YSLEpDepoMvm0OoJbkJacx03iAdy25ZUtxjpY-wqxTzHlPZ4ltyNrg04buneUF-f7_6dfmjWd9c_7z8tm48b6VpOi81V1K3Xgvt27bVCkBgZ4QwHpRn0ksl-0GojkNQohdKdAIkQq8CD4O4IF-PvttdP2LwmOfqkt3WOLp6sMVF-7-S48belr1lbMkSejH4-GRQy58dTrMd4-QxJZdx-c8aqQyTii3gpyPoa5mmisMphIH91409dbOwH55fdSKPZYgHypeLfQ</recordid><startdate>19790215</startdate><enddate>19790215</enddate><creator>Tamulevicius, P</creator><creator>Streffer, C</creator><creator>Roscic, O</creator><creator>Hubert, E</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>19790215</creationdate><title>Localization of oxidized nocotinamide--adenine dinucleotide glycohydrolase in the mouse liver nuclear envelope</title><author>Tamulevicius, P ; Streffer, C ; Roscic, O ; Hubert, E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c2847-9c4625468c636c88865003e97337c05c14c454bf35920d53b3539304e0b5d2df3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1979</creationdate><topic>Animals</topic><topic>Chromatin - enzymology</topic><topic>Deoxyribonucleases - pharmacology</topic><topic>Glucose-6-Phosphatase - metabolism</topic><topic>In Vitro Techniques</topic><topic>Liver - enzymology</topic><topic>Liver - ultrastructure</topic><topic>Male</topic><topic>Mice</topic><topic>Microscopy, Electron</topic><topic>NAD+ Nucleosidase - metabolism</topic><topic>Nuclear Envelope - drug effects</topic><topic>Nuclear Envelope - enzymology</topic><topic>Nuclear Envelope - ultrastructure</topic><topic>Phospholipases - pharmacology</topic><topic>Phospholipids - metabolism</topic><topic>Polyethylene Glycols - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tamulevicius, P</creatorcontrib><creatorcontrib>Streffer, C</creatorcontrib><creatorcontrib>Roscic, O</creatorcontrib><creatorcontrib>Hubert, E</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>Tamulevicius, P</au><au>Streffer, C</au><au>Roscic, O</au><au>Hubert, E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Localization of oxidized nocotinamide--adenine dinucleotide glycohydrolase in the mouse liver nuclear envelope</atitle><jtitle>Biochemical journal</jtitle><addtitle>Biochem J</addtitle><date>1979-02-15</date><risdate>1979</risdate><volume>178</volume><issue>2</issue><spage>467</spage><epage>473</epage><pages>467-473</pages><issn>0264-6021</issn><issn>0306-3283</issn><eissn>1470-8728</eissn><abstract>NAD+ glycohydrolase activity located in the nuclear envelope was maximally solubilized by treatment with 0.1--0.2% Triton X-100. The residual activity largely represents the chromatin-associated NAD+ glycohydrolase. Under these conditions the phospholipids were extensively solubilized (over 90%) while leaving the nuclei physically stable, although the nuclear membranes were removed, as shown by electron microscopy. After Triton X-100 treatment, deoxyribonuclease I did not significantly affect the residual NAD+ glycohydrolase activity, although the DNA was completely broken down. This enzyme activity can be released from the nuclear pellet by incubation with phospholipase C. For comparative studies, the glucose 6-phosphatase activity, known to be present in the nuclear envelope, was investigated. Treatment with 0.01% Triton X-100 released 10--20% of the phospholipids, but without solubilizing either glucose 6-phosphatase or NAD+ glycohydrolase. Higher Triton X-100 concentrations (0.1--1.0%) inhibited glucose 6-phosphatase, but not NAD+ glycohydrolase activity. NAD+ glycohydrolase is apparently present in a latent form in the nuclear envelope. Glucose 6-phosphatase, However, shows no such latency.</abstract><cop>England</cop><pmid>220967</pmid><doi>10.1042/bj1780467</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Animals Chromatin - enzymology Deoxyribonucleases - pharmacology Glucose-6-Phosphatase - metabolism In Vitro Techniques Liver - enzymology Liver - ultrastructure Male Mice Microscopy, Electron NAD+ Nucleosidase - metabolism Nuclear Envelope - drug effects Nuclear Envelope - enzymology Nuclear Envelope - ultrastructure Phospholipases - pharmacology Phospholipids - metabolism Polyethylene Glycols - pharmacology |
title | Localization of oxidized nocotinamide--adenine dinucleotide glycohydrolase in the mouse liver nuclear envelope |
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