Interaction of nogalamycin with chromatin
Number of available nogalamycin binding sites in Sarcoma-180 chromatin is less than that present in Sarcoma-180 DNA. Gradual removal of proteins from chromatin by salt leads to increase in available drug binding sites, without appreciable alteration in binding affinity. Histones restrict the accessi...
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| Veröffentlicht in: | Chemico-biological interactions 1983-01, Vol.46 (3), p.347-352 |
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| container_end_page | 352 |
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| container_issue | 3 |
| container_start_page | 347 |
| container_title | Chemico-biological interactions |
| container_volume | 46 |
| creator | Ganguli, Runu Chowdhury, Kanakendu Chakbaborty, Bimal Neogy, Rajat K. |
| description | Number of available nogalamycin binding sites in Sarcoma-180 chromatin is less than that present in Sarcoma-180 DNA. Gradual removal of proteins from chromatin by salt leads to increase in available drug binding sites, without appreciable alteration in binding affinity. Histones restrict the accessibility of nogalamycin to chromosomal DNA, whereas high mobility group (HMG) proteins have no effect. Association of histone H1 with chromosomal DNA has a more marked inhibitory effect on nogalamycin binding than other types of histones. Chromosomal protein induced conformational change in DNA appears to be the main factor in determining the availability of strong binding sites. |
| doi_str_mv | 10.1016/0009-2797(83)90018-2 |
| format | Article |
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Gradual removal of proteins from chromatin by salt leads to increase in available drug binding sites, without appreciable alteration in binding affinity. Histones restrict the accessibility of nogalamycin to chromosomal DNA, whereas high mobility group (HMG) proteins have no effect. Association of histone H1 with chromosomal DNA has a more marked inhibitory effect on nogalamycin binding than other types of histones. Chromosomal protein induced conformational change in DNA appears to be the main factor in determining the availability of strong binding sites.</description><identifier>ISSN: 0009-2797</identifier><identifier>EISSN: 1872-7786</identifier><identifier>DOI: 10.1016/0009-2797(83)90018-2</identifier><identifier>PMID: 6640781</identifier><identifier>CODEN: CBINA8</identifier><language>eng</language><publisher>Shannon: Elsevier Ireland Ltd</publisher><subject>Anthracycline ; Antineoplastic agents ; Biological and medical sciences ; Chemotherapy ; Chromatin ; Chromatin - metabolism ; Chromosomal Proteins, Non-Histone - pharmacology ; Daunorubicin - analogs & derivatives ; Drug Interactions ; Histones ; Interaction ; Medical sciences ; Nogalamycin - metabolism ; Pharmacology. 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Gradual removal of proteins from chromatin by salt leads to increase in available drug binding sites, without appreciable alteration in binding affinity. Histones restrict the accessibility of nogalamycin to chromosomal DNA, whereas high mobility group (HMG) proteins have no effect. Association of histone H1 with chromosomal DNA has a more marked inhibitory effect on nogalamycin binding than other types of histones. Chromosomal protein induced conformational change in DNA appears to be the main factor in determining the availability of strong binding sites.</description><subject>Anthracycline</subject><subject>Antineoplastic agents</subject><subject>Biological and medical sciences</subject><subject>Chemotherapy</subject><subject>Chromatin</subject><subject>Chromatin - metabolism</subject><subject>Chromosomal Proteins, Non-Histone - pharmacology</subject><subject>Daunorubicin - analogs & derivatives</subject><subject>Drug Interactions</subject><subject>Histones</subject><subject>Interaction</subject><subject>Medical sciences</subject><subject>Nogalamycin - metabolism</subject><subject>Pharmacology. 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Drug treatments</topic><topic>Protein Binding</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ganguli, Runu</creatorcontrib><creatorcontrib>Chowdhury, Kanakendu</creatorcontrib><creatorcontrib>Chakbaborty, Bimal</creatorcontrib><creatorcontrib>Neogy, Rajat K.</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>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>Chemico-biological interactions</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ganguli, Runu</au><au>Chowdhury, Kanakendu</au><au>Chakbaborty, Bimal</au><au>Neogy, Rajat K.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interaction of nogalamycin with chromatin</atitle><jtitle>Chemico-biological interactions</jtitle><addtitle>Chem Biol Interact</addtitle><date>1983-01-01</date><risdate>1983</risdate><volume>46</volume><issue>3</issue><spage>347</spage><epage>352</epage><pages>347-352</pages><issn>0009-2797</issn><eissn>1872-7786</eissn><coden>CBINA8</coden><abstract>Number of available nogalamycin binding sites in Sarcoma-180 chromatin is less than that present in Sarcoma-180 DNA. Gradual removal of proteins from chromatin by salt leads to increase in available drug binding sites, without appreciable alteration in binding affinity. Histones restrict the accessibility of nogalamycin to chromosomal DNA, whereas high mobility group (HMG) proteins have no effect. Association of histone H1 with chromosomal DNA has a more marked inhibitory effect on nogalamycin binding than other types of histones. Chromosomal protein induced conformational change in DNA appears to be the main factor in determining the availability of strong binding sites.</abstract><cop>Shannon</cop><pub>Elsevier Ireland Ltd</pub><pmid>6640781</pmid><doi>10.1016/0009-2797(83)90018-2</doi><tpages>6</tpages></addata></record> |
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| ispartof | Chemico-biological interactions, 1983-01, Vol.46 (3), p.347-352 |
| issn | 0009-2797 1872-7786 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Anthracycline Antineoplastic agents Biological and medical sciences Chemotherapy Chromatin Chromatin - metabolism Chromosomal Proteins, Non-Histone - pharmacology Daunorubicin - analogs & derivatives Drug Interactions Histones Interaction Medical sciences Nogalamycin - metabolism Pharmacology. Drug treatments Protein Binding |
| title | Interaction of nogalamycin with chromatin |
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