Preliminary characterization of chelation-sensitive nucleoprotein particles
Nucleoprotein particles (B2), isolated following digestion of calf thymus chromatin with micrococcal nuclease, are resolved on a non-chelating Bio-Gel A-5m column. B2 protein electrophoresis showed the presence of several H1 species and several nonhistone proteins but was depleted in core histones....
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| Veröffentlicht in: | Biochemical and biophysical research communications 1982-01, Vol.104 (2), p.491-499 |
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| container_issue | 2 |
| container_start_page | 491 |
| container_title | Biochemical and biophysical research communications |
| container_volume | 104 |
| creator | Beary, David A. Vizard, Douglas L. LaBiche, Ronald A. Hardy, Kenneth J. Bryan, Sara E. |
| description | Nucleoprotein particles (B2), isolated following digestion of calf thymus chromatin with micrococcal nuclease, are resolved on a non-chelating Bio-Gel A-5m column. B2 protein electrophoresis showed the presence of several H1 species and several nonhistone proteins but was depleted in core histones. DNA electrophoresis demonstrated that native B2 DNA has a length of about 46 base pairs. On DNA sequencing gels, the length distribution of denatured B2 DNA ranged from 12 to 35 bases with a weighted average chain length of about 26 bases. Depletion of a 20 base band in B2 DNA suggested specific protection of internucleosomal DNA sites during the nuclease digestion. |
| doi_str_mv | 10.1016/0006-291X(82)90663-5 |
| format | Article |
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B2 protein electrophoresis showed the presence of several H1 species and several nonhistone proteins but was depleted in core histones. DNA electrophoresis demonstrated that native B2 DNA has a length of about 46 base pairs. On DNA sequencing gels, the length distribution of denatured B2 DNA ranged from 12 to 35 bases with a weighted average chain length of about 26 bases. Depletion of a 20 base band in B2 DNA suggested specific protection of internucleosomal DNA sites during the nuclease digestion.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/0006-291X(82)90663-5</identifier><identifier>PMID: 6803783</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; calf thymus ; Cattle ; chromatin ; Chromatin - analysis ; Chromosomal Proteins, Non-Histone - isolation & purification ; Deoxyribonucleoproteins - isolation & purification ; DNA ; DNA - isolation & purification ; Edetic Acid ; Electrophoresis, Polyacrylamide Gel ; fractionation ; Histones - isolation & purification ; Micrococcal Nuclease ; Molecular Weight ; nucleoproteins ; Nucleoproteins - isolation & purification ; Thymus Gland - analysis</subject><ispartof>Biochemical and biophysical research communications, 1982-01, Vol.104 (2), p.491-499</ispartof><rights>1982</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c388t-51fcbf14badf895c54d00b499f1ebd72f9840fc34548e9e17ed413f651568073</citedby><cites>FETCH-LOGICAL-c388t-51fcbf14badf895c54d00b499f1ebd72f9840fc34548e9e17ed413f651568073</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0006-291X(82)90663-5$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6803783$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Beary, David A.</creatorcontrib><creatorcontrib>Vizard, Douglas L.</creatorcontrib><creatorcontrib>LaBiche, Ronald A.</creatorcontrib><creatorcontrib>Hardy, Kenneth J.</creatorcontrib><creatorcontrib>Bryan, Sara E.</creatorcontrib><title>Preliminary characterization of chelation-sensitive nucleoprotein particles</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Nucleoprotein particles (B2), isolated following digestion of calf thymus chromatin with micrococcal nuclease, are resolved on a non-chelating Bio-Gel A-5m column. B2 protein electrophoresis showed the presence of several H1 species and several nonhistone proteins but was depleted in core histones. DNA electrophoresis demonstrated that native B2 DNA has a length of about 46 base pairs. On DNA sequencing gels, the length distribution of denatured B2 DNA ranged from 12 to 35 bases with a weighted average chain length of about 26 bases. Depletion of a 20 base band in B2 DNA suggested specific protection of internucleosomal DNA sites during the nuclease digestion.</description><subject>Animals</subject><subject>calf thymus</subject><subject>Cattle</subject><subject>chromatin</subject><subject>Chromatin - analysis</subject><subject>Chromosomal Proteins, Non-Histone - isolation & purification</subject><subject>Deoxyribonucleoproteins - isolation & purification</subject><subject>DNA</subject><subject>DNA - isolation & purification</subject><subject>Edetic Acid</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>fractionation</subject><subject>Histones - isolation & purification</subject><subject>Micrococcal Nuclease</subject><subject>Molecular Weight</subject><subject>nucleoproteins</subject><subject>Nucleoproteins - isolation & purification</subject><subject>Thymus Gland - analysis</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1982</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1LxDAQhoMoun78A4U9iR6qM22SJhdBFr9wQQ978BbadIKRbrsmXUF_vVl38ainYWbe953hYewY4QIB5SUAyCzX-HKm8nMNUhaZ2GIjBA1ZjsC32ehXssf2Y3wDQORS77JdqaAoVTFij8-BWj_3XRU-x_a1CpUdKPivavB9N-5dmlH702SRuugH_0Hjbmlb6hehH8h340UVBp8G8ZDtuKqNdLSpB2x2ezOb3GfTp7uHyfU0s4VSQybQ2dohr6vGKS2s4A1AzbV2SHVT5k4rDs4WXHBFmrCkhmPhpECR3i6LA3a6jk0PvC8pDmbuo6W2rTrql9GUHHLBhfpXiILnSkpMQr4W2tDHGMiZRfDzRMQgmBVrswJpViCNys0PayOS7WSTv6zn1PyaNnDT_mq9pwTjw1Mw0XrqLDU-kB1M0_u_D3wDuWiPSQ</recordid><startdate>19820101</startdate><enddate>19820101</enddate><creator>Beary, David A.</creator><creator>Vizard, Douglas L.</creator><creator>LaBiche, Ronald A.</creator><creator>Hardy, Kenneth J.</creator><creator>Bryan, Sara E.</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>7TM</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19820101</creationdate><title>Preliminary characterization of chelation-sensitive nucleoprotein particles</title><author>Beary, David A. ; Vizard, Douglas L. ; LaBiche, Ronald A. ; Hardy, Kenneth J. ; Bryan, Sara E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c388t-51fcbf14badf895c54d00b499f1ebd72f9840fc34548e9e17ed413f651568073</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1982</creationdate><topic>Animals</topic><topic>calf thymus</topic><topic>Cattle</topic><topic>chromatin</topic><topic>Chromatin - analysis</topic><topic>Chromosomal Proteins, Non-Histone - isolation & purification</topic><topic>Deoxyribonucleoproteins - isolation & purification</topic><topic>DNA</topic><topic>DNA - isolation & purification</topic><topic>Edetic Acid</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>fractionation</topic><topic>Histones - isolation & purification</topic><topic>Micrococcal Nuclease</topic><topic>Molecular Weight</topic><topic>nucleoproteins</topic><topic>Nucleoproteins - isolation & purification</topic><topic>Thymus Gland - analysis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Beary, David A.</creatorcontrib><creatorcontrib>Vizard, Douglas L.</creatorcontrib><creatorcontrib>LaBiche, Ronald A.</creatorcontrib><creatorcontrib>Hardy, Kenneth J.</creatorcontrib><creatorcontrib>Bryan, Sara 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>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Environmental Sciences and Pollution Management</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>Beary, David A.</au><au>Vizard, Douglas L.</au><au>LaBiche, Ronald A.</au><au>Hardy, Kenneth J.</au><au>Bryan, Sara E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Preliminary characterization of chelation-sensitive nucleoprotein particles</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1982-01-01</date><risdate>1982</risdate><volume>104</volume><issue>2</issue><spage>491</spage><epage>499</epage><pages>491-499</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Nucleoprotein particles (B2), isolated following digestion of calf thymus chromatin with micrococcal nuclease, are resolved on a non-chelating Bio-Gel A-5m column. B2 protein electrophoresis showed the presence of several H1 species and several nonhistone proteins but was depleted in core histones. DNA electrophoresis demonstrated that native B2 DNA has a length of about 46 base pairs. On DNA sequencing gels, the length distribution of denatured B2 DNA ranged from 12 to 35 bases with a weighted average chain length of about 26 bases. Depletion of a 20 base band in B2 DNA suggested specific protection of internucleosomal DNA sites during the nuclease digestion.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>6803783</pmid><doi>10.1016/0006-291X(82)90663-5</doi><tpages>9</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 1982-01, Vol.104 (2), p.491-499 |
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| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Animals calf thymus Cattle chromatin Chromatin - analysis Chromosomal Proteins, Non-Histone - isolation & purification Deoxyribonucleoproteins - isolation & purification DNA DNA - isolation & purification Edetic Acid Electrophoresis, Polyacrylamide Gel fractionation Histones - isolation & purification Micrococcal Nuclease Molecular Weight nucleoproteins Nucleoproteins - isolation & purification Thymus Gland - analysis |
| title | Preliminary characterization of chelation-sensitive nucleoprotein particles |
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