Nucleolin (C23), a physiological substrate for casein kinase II
Nucleolin (C23), a 110 kDa phosphoprotein, which is mainly found in the nucleolus has been shown to be a physiological substrate for casein kinase II (CKII). Nucleolin was identified and characterized by immunodetection using an anti-nucleolin antibody. Phosphopeptide patterns from nucleolin phospho...
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Veröffentlicht in: | Biochemical and biophysical research communications 1988-11, Vol.156 (3), p.1390-1397 |
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description | Nucleolin (C23), a 110 kDa phosphoprotein, which is mainly found in the nucleolus has been shown to be a physiological substrate for casein kinase II (CKII). Nucleolin was identified and characterized by immunodetection using an anti-nucleolin antibody. Phosphopeptide patterns from nucleolin phosphorylated by purified casein kinase II and of phosphorylated nucleolin which had been isolated from tumor cells grown in the presence of [
32P]-o-phosphate, were identical. The partial tryptic digest revealed nine phosphopeptides. Nucleolin isolated from Krebs II mouse ascites cells was phosphorylated by purified casein kinase II with about two moles phosphate per one mole of nucleolin. |
doi_str_mv | 10.1016/S0006-291X(88)80786-1 |
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32P]-o-phosphate, were identical. The partial tryptic digest revealed nine phosphopeptides. Nucleolin isolated from Krebs II mouse ascites cells was phosphorylated by purified casein kinase II with about two moles phosphate per one mole of nucleolin.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/S0006-291X(88)80786-1</identifier><identifier>PMID: 3190709</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Carcinoma, Ehrlich Tumor - analysis ; casein kinase II ; Casein Kinases ; Mice ; Nuclear Proteins - metabolism ; Nucleolin ; Phosphoproteins - metabolism ; Phosphorylation ; Protein Kinases - metabolism ; RNA-Binding Proteins</subject><ispartof>Biochemical and biophysical research communications, 1988-11, Vol.156 (3), p.1390-1397</ispartof><rights>1988 Academic Press, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c391t-8362b63df384607fd9fc114facb988551acf8df77ee7c3bc0743273952b584743</citedby><cites>FETCH-LOGICAL-c391t-8362b63df384607fd9fc114facb988551acf8df77ee7c3bc0743273952b584743</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006291X88807861$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3190709$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Schneider, Helge R.</creatorcontrib><creatorcontrib>Issinger, Olaf-Georg</creatorcontrib><title>Nucleolin (C23), a physiological substrate for casein kinase II</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Nucleolin (C23), a 110 kDa phosphoprotein, which is mainly found in the nucleolus has been shown to be a physiological substrate for casein kinase II (CKII). Nucleolin was identified and characterized by immunodetection using an anti-nucleolin antibody. Phosphopeptide patterns from nucleolin phosphorylated by purified casein kinase II and of phosphorylated nucleolin which had been isolated from tumor cells grown in the presence of [
32P]-o-phosphate, were identical. The partial tryptic digest revealed nine phosphopeptides. Nucleolin isolated from Krebs II mouse ascites cells was phosphorylated by purified casein kinase II with about two moles phosphate per one mole of nucleolin.</description><subject>Animals</subject><subject>Carcinoma, Ehrlich Tumor - analysis</subject><subject>casein kinase II</subject><subject>Casein Kinases</subject><subject>Mice</subject><subject>Nuclear Proteins - metabolism</subject><subject>Nucleolin</subject><subject>Phosphoproteins - metabolism</subject><subject>Phosphorylation</subject><subject>Protein Kinases - metabolism</subject><subject>RNA-Binding Proteins</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtLAzEQgIMotVZ_QmFP0oKrk81mk5yKFB-FogcVvIVsNtHotluTXaH_3vSB155mhvnmwYfQEMM1BlzcvABAkWYCv484H3NgvEjxEepjEJBmGPJj1P9HTtFZCF8AGOeF6KEewQIYiD6aPHW6Nk3tlslompHxVaKS1ec6uKZuPpxWdRK6MrRetSaxjU-0Ciay324Zk2Q2O0cnVtXBXOzjAL3d371OH9P588NsejtPNRG4TTkpsrIglSU8L4DZSlgdf7FKl4JzSrHSlleWMWOYJqUGlpOMEUGzkvI8FgN0udu78s1PZ0IrFy5oU9dqaZouSMYpKSghB0FMgYv4RQTpDtS-CcEbK1feLZRfSwxyY1huDcuNPsm53BqWOM4N9we6cmGq_6m90tif7Pom6vh1xsugnVlqUzlvdCurxh248Ad_4Ijn</recordid><startdate>19881115</startdate><enddate>19881115</enddate><creator>Schneider, Helge R.</creator><creator>Issinger, Olaf-Georg</creator><general>Elsevier Inc</general><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>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19881115</creationdate><title>Nucleolin (C23), a physiological substrate for casein kinase II</title><author>Schneider, Helge R. ; Issinger, Olaf-Georg</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c391t-8362b63df384607fd9fc114facb988551acf8df77ee7c3bc0743273952b584743</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>Animals</topic><topic>Carcinoma, Ehrlich Tumor - analysis</topic><topic>casein kinase II</topic><topic>Casein Kinases</topic><topic>Mice</topic><topic>Nuclear Proteins - metabolism</topic><topic>Nucleolin</topic><topic>Phosphoproteins - metabolism</topic><topic>Phosphorylation</topic><topic>Protein Kinases - metabolism</topic><topic>RNA-Binding Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schneider, Helge R.</creatorcontrib><creatorcontrib>Issinger, Olaf-Georg</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schneider, Helge R.</au><au>Issinger, Olaf-Georg</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Nucleolin (C23), a physiological substrate for casein kinase II</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1988-11-15</date><risdate>1988</risdate><volume>156</volume><issue>3</issue><spage>1390</spage><epage>1397</epage><pages>1390-1397</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Nucleolin (C23), a 110 kDa phosphoprotein, which is mainly found in the nucleolus has been shown to be a physiological substrate for casein kinase II (CKII). Nucleolin was identified and characterized by immunodetection using an anti-nucleolin antibody. Phosphopeptide patterns from nucleolin phosphorylated by purified casein kinase II and of phosphorylated nucleolin which had been isolated from tumor cells grown in the presence of [
32P]-o-phosphate, were identical. The partial tryptic digest revealed nine phosphopeptides. Nucleolin isolated from Krebs II mouse ascites cells was phosphorylated by purified casein kinase II with about two moles phosphate per one mole of nucleolin.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>3190709</pmid><doi>10.1016/S0006-291X(88)80786-1</doi><tpages>8</tpages></addata></record> |
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subjects | Animals Carcinoma, Ehrlich Tumor - analysis casein kinase II Casein Kinases Mice Nuclear Proteins - metabolism Nucleolin Phosphoproteins - metabolism Phosphorylation Protein Kinases - metabolism RNA-Binding Proteins |
title | Nucleolin (C23), a physiological substrate for casein kinase II |
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