In vitro phosphorylation of proteins tightly bound to DNA by protein kinase NII
1. 1. Highly purified DNA from calf thymus was phosphorylated with protein kinase NII. 2. 2. Digestion with proteinase K of this DNA demonstrates proteins as phosphorylated component. 3. 3. Gel filtration chromatography on Bio-Gel A-0.5m gel column shows a major protein peak between 50 and 70 kDa. 4...
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| Veröffentlicht in: | International journal of biochemistry 1993-07, Vol.25 (7), p.1035-1039 |
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| container_end_page | 1039 |
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| container_issue | 7 |
| container_start_page | 1035 |
| container_title | International journal of biochemistry |
| container_volume | 25 |
| creator | Piccinini, Gina Bramucci, Massimo Maccari, Ennio Miano, Antonino Amici, Domenico Gianfranceschi, Gian Luigi Cardellini, Elena |
| description | 1.
1. Highly purified DNA from calf thymus was phosphorylated with protein kinase NII.
2.
2. Digestion with proteinase K of this DNA demonstrates proteins as phosphorylated component.
3.
3. Gel filtration chromatography on Bio-Gel A-0.5m gel column shows a major protein peak between 50 and 70 kDa.
4.
4. SDS gel electrophoresis, after hydrolysis, to digest completely DNA, shows three major phosphorylated bands corresponding to polypeptides of Mr between 31 and 21 kDa.
5.
5. After high voltage electrophoresis on TLC plates tryptic digested polypeptides show very similar phosphopeptides patterns. |
| doi_str_mv | 10.1016/0020-711X(93)90118-X |
| format | Article |
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1. Highly purified DNA from calf thymus was phosphorylated with protein kinase NII.
2.
2. Digestion with proteinase K of this DNA demonstrates proteins as phosphorylated component.
3.
3. Gel filtration chromatography on Bio-Gel A-0.5m gel column shows a major protein peak between 50 and 70 kDa.
4.
4. SDS gel electrophoresis, after hydrolysis, to digest completely DNA, shows three major phosphorylated bands corresponding to polypeptides of Mr between 31 and 21 kDa.
5.
5. After high voltage electrophoresis on TLC plates tryptic digested polypeptides show very similar phosphopeptides patterns.</description><identifier>ISSN: 0020-711X</identifier><identifier>DOI: 10.1016/0020-711X(93)90118-X</identifier><identifier>PMID: 8365545</identifier><language>eng</language><publisher>Oxford: Elsevier B.V</publisher><subject>Analytical, structural and metabolic biochemistry ; Animals ; Binding and carrier proteins ; Biological and medical sciences ; Caseins - metabolism ; Cattle ; Chromatography, Gel ; Chromatography, Thin Layer ; DNA - metabolism ; DNA-Binding Proteins - metabolism ; Electrophoresis, Polyacrylamide Gel ; Fundamental and applied biological sciences. Psychology ; Phosphorylation ; Protein Kinases - metabolism ; Proteins ; Substrate Specificity</subject><ispartof>International journal of biochemistry, 1993-07, Vol.25 (7), p.1035-1039</ispartof><rights>1993</rights><rights>1993 INIST-CNRS</rights><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c366t-7fee08e5cf9f1211986804736a95cb99be3205a060e04ea427323fa4d37ba1ae3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4857853$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8365545$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Piccinini, Gina</creatorcontrib><creatorcontrib>Bramucci, Massimo</creatorcontrib><creatorcontrib>Maccari, Ennio</creatorcontrib><creatorcontrib>Miano, Antonino</creatorcontrib><creatorcontrib>Amici, Domenico</creatorcontrib><creatorcontrib>Gianfranceschi, Gian Luigi</creatorcontrib><creatorcontrib>Cardellini, Elena</creatorcontrib><title>In vitro phosphorylation of proteins tightly bound to DNA by protein kinase NII</title><title>International journal of biochemistry</title><addtitle>Int J Biochem</addtitle><description>1.
1. Highly purified DNA from calf thymus was phosphorylated with protein kinase NII.
2.
2. Digestion with proteinase K of this DNA demonstrates proteins as phosphorylated component.
3.
3. Gel filtration chromatography on Bio-Gel A-0.5m gel column shows a major protein peak between 50 and 70 kDa.
4.
4. SDS gel electrophoresis, after hydrolysis, to digest completely DNA, shows three major phosphorylated bands corresponding to polypeptides of Mr between 31 and 21 kDa.
5.
5. After high voltage electrophoresis on TLC plates tryptic digested polypeptides show very similar phosphopeptides patterns.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Binding and carrier proteins</subject><subject>Biological and medical sciences</subject><subject>Caseins - metabolism</subject><subject>Cattle</subject><subject>Chromatography, Gel</subject><subject>Chromatography, Thin Layer</subject><subject>DNA - metabolism</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Phosphorylation</subject><subject>Protein Kinases - metabolism</subject><subject>Proteins</subject><subject>Substrate Specificity</subject><issn>0020-711X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1PGzEQhn2gojTwD0DyoUJw2GKvP9a-IKGUlkgRXEDKzfJ6Z4vLZp3a3kj59900IUd6GI0088zo1YPQOSXfKKHyhpCSFBWliyvNrjWhVBWLI3RyGH9GX1L6TQjVitNjdKyYFIKLE_Q06_Ha5xjw6jWkseKms9mHHocWr2LI4PuEs__1mrsNrsPQNzgH_P3xDtebdwC_-d4mwI-z2Sn61Nouwdm-T9DLj_vn6UMxf_o5m97NC8ekzEXVAhAFwrW6pSUdY0lFeMWk1cLVWtfASiIskQQIB8vLipWstbxhVW2pBTZBl7u_Y4Q_A6Rslj456DrbQxiSqYRmTCv1X5BKySom-AjyHehiSClCa1bRL23cGErMVrLZ2jRbm0Yz80-yWYxnF_v_Q72E5nC0Nzzuv-73NjnbtdH2zqcDxpWolGAjdrvDYJS29hBNch56B42P4LJpgv84x18y0Zn6</recordid><startdate>19930701</startdate><enddate>19930701</enddate><creator>Piccinini, Gina</creator><creator>Bramucci, Massimo</creator><creator>Maccari, Ennio</creator><creator>Miano, Antonino</creator><creator>Amici, Domenico</creator><creator>Gianfranceschi, Gian Luigi</creator><creator>Cardellini, Elena</creator><general>Elsevier B.V</general><general>Pergamon</general><scope>IQODW</scope><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>7TM</scope><scope>7X8</scope></search><sort><creationdate>19930701</creationdate><title>In vitro phosphorylation of proteins tightly bound to DNA by protein kinase NII</title><author>Piccinini, Gina ; Bramucci, Massimo ; Maccari, Ennio ; Miano, Antonino ; Amici, Domenico ; Gianfranceschi, Gian Luigi ; Cardellini, Elena</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c366t-7fee08e5cf9f1211986804736a95cb99be3205a060e04ea427323fa4d37ba1ae3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Binding and carrier proteins</topic><topic>Biological and medical sciences</topic><topic>Caseins - metabolism</topic><topic>Cattle</topic><topic>Chromatography, Gel</topic><topic>Chromatography, Thin Layer</topic><topic>DNA - metabolism</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Phosphorylation</topic><topic>Protein Kinases - metabolism</topic><topic>Proteins</topic><topic>Substrate Specificity</topic><toplevel>online_resources</toplevel><creatorcontrib>Piccinini, Gina</creatorcontrib><creatorcontrib>Bramucci, Massimo</creatorcontrib><creatorcontrib>Maccari, Ennio</creatorcontrib><creatorcontrib>Miano, Antonino</creatorcontrib><creatorcontrib>Amici, Domenico</creatorcontrib><creatorcontrib>Gianfranceschi, Gian Luigi</creatorcontrib><creatorcontrib>Cardellini, Elena</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>International journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Piccinini, Gina</au><au>Bramucci, Massimo</au><au>Maccari, Ennio</au><au>Miano, Antonino</au><au>Amici, Domenico</au><au>Gianfranceschi, Gian Luigi</au><au>Cardellini, Elena</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>In vitro phosphorylation of proteins tightly bound to DNA by protein kinase NII</atitle><jtitle>International journal of biochemistry</jtitle><addtitle>Int J Biochem</addtitle><date>1993-07-01</date><risdate>1993</risdate><volume>25</volume><issue>7</issue><spage>1035</spage><epage>1039</epage><pages>1035-1039</pages><issn>0020-711X</issn><abstract>1.
1. Highly purified DNA from calf thymus was phosphorylated with protein kinase NII.
2.
2. Digestion with proteinase K of this DNA demonstrates proteins as phosphorylated component.
3.
3. Gel filtration chromatography on Bio-Gel A-0.5m gel column shows a major protein peak between 50 and 70 kDa.
4.
4. SDS gel electrophoresis, after hydrolysis, to digest completely DNA, shows three major phosphorylated bands corresponding to polypeptides of Mr between 31 and 21 kDa.
5.
5. After high voltage electrophoresis on TLC plates tryptic digested polypeptides show very similar phosphopeptides patterns.</abstract><cop>Oxford</cop><pub>Elsevier B.V</pub><pmid>8365545</pmid><doi>10.1016/0020-711X(93)90118-X</doi><tpages>5</tpages></addata></record> |
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| ispartof | International journal of biochemistry, 1993-07, Vol.25 (7), p.1035-1039 |
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| language | eng |
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| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Analytical, structural and metabolic biochemistry Animals Binding and carrier proteins Biological and medical sciences Caseins - metabolism Cattle Chromatography, Gel Chromatography, Thin Layer DNA - metabolism DNA-Binding Proteins - metabolism Electrophoresis, Polyacrylamide Gel Fundamental and applied biological sciences. Psychology Phosphorylation Protein Kinases - metabolism Proteins Substrate Specificity |
| title | In vitro phosphorylation of proteins tightly bound to DNA by protein kinase NII |
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