MECHANISM OF ACTION OF ACLACINOMYCIN A II. THE INTERACTION WITH DNA AND WITH TUBULIN
Aclacinomycin A was observed to effect the thermal denaturation of DNA and to increase Tm. The visible absorption spectrum of the antibiotic showed bathochromic and hypochromic shifts upon reaction with native and heat-denatured DNA. [14C]Aclacinomycin A was demonstrated by equilibrium dialysis to b...
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| Veröffentlicht in: | Journal of antibiotics 1979, Vol.32(1), pp.48-52 |
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| container_title | Journal of antibiotics |
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| creator | MISUMI, MASAROU YAMAKI, HIROSHI AKIYAMA, TETSU TANAKA, NOBUO |
| description | Aclacinomycin A was observed to effect the thermal denaturation of DNA and to increase Tm. The visible absorption spectrum of the antibiotic showed bathochromic and hypochromic shifts upon reaction with native and heat-denatured DNA. [14C]Aclacinomycin A was demonstrated by equilibrium dialysis to bind to DNA. Native calf thymus DNA appeared to possess one binding site per ca. 6 nucleotides for the antibiotic with an apparent association constant of ca. 1.2×106 M-1. Heat-denatured DNA showed much less affinity for the antibiotic: one binding site per ca. 6 nucleotides with an apparent binding constant of ca. 3.5×104 M-1. The difference of association constants between double- and single-stranded DNAs suggested that the antibiotic may be intercalated between base pairs of the DNA double helix. [14C]Aclacinomycin A exhibited higher affinity for poly(dAdT) than for poly(dIdC). The antibiotic showed a significant difference spectrum with porcine tubulin, indicating an interaction with tubulin. The binding to tubulin was also demonstrated by equilibrium dialysis of [14C]aclacinomycin A and tubulin. |
| doi_str_mv | 10.7164/antibiotics.32.48 |
| format | Article |
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The difference of association constants between double- and single-stranded DNAs suggested that the antibiotic may be intercalated between base pairs of the DNA double helix. [14C]Aclacinomycin A exhibited higher affinity for poly(dAdT) than for poly(dIdC). The antibiotic showed a significant difference spectrum with porcine tubulin, indicating an interaction with tubulin. 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THE INTERACTION WITH DNA AND WITH TUBULIN</title><title>Journal of antibiotics</title><addtitle>J. Antibiot.</addtitle><description>Aclacinomycin A was observed to effect the thermal denaturation of DNA and to increase Tm. The visible absorption spectrum of the antibiotic showed bathochromic and hypochromic shifts upon reaction with native and heat-denatured DNA. [14C]Aclacinomycin A was demonstrated by equilibrium dialysis to bind to DNA. Native calf thymus DNA appeared to possess one binding site per ca. 6 nucleotides for the antibiotic with an apparent association constant of ca. 1.2×106 M-1. Heat-denatured DNA showed much less affinity for the antibiotic: one binding site per ca. 6 nucleotides with an apparent binding constant of ca. 3.5×104 M-1. The difference of association constants between double- and single-stranded DNAs suggested that the antibiotic may be intercalated between base pairs of the DNA double helix. [14C]Aclacinomycin A exhibited higher affinity for poly(dAdT) than for poly(dIdC). The antibiotic showed a significant difference spectrum with porcine tubulin, indicating an interaction with tubulin. The binding to tubulin was also demonstrated by equilibrium dialysis of [14C]aclacinomycin A and tubulin.</description><subject>Antibiotics, Antineoplastic - metabolism</subject><subject>Chemical Phenomena</subject><subject>Chemistry</subject><subject>Dialysis</subject><subject>DNA - metabolism</subject><subject>Glycoproteins - metabolism</subject><subject>Hot Temperature</subject><subject>Naphthacenes - metabolism</subject><subject>Nucleic Acid Denaturation</subject><subject>Polydeoxyribonucleotides - metabolism</subject><subject>Protein Binding</subject><subject>Tubulin - metabolism</subject><issn>0021-8820</issn><issn>1881-1469</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1979</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpNkF9PwjAUxRvjP0Q_gIkPe_Jt2NuWrnucY0gNbImOGJ-arnQ6AwxXePDbOzJCeLn3NuecX9KD0D3gQQCcPen1tiqqelsZN6BkwMQZ6oEQ4APj4TnqYUzAF4Lga3Tj3A_GNKCBuEKXAYcwJD2Uz5J4EqXyfeZlYy-Kc5ml3TWNYplms892epEn5cDLJ4kn0zx5O9g-ZD7xRmnkRemoe-Tz5_lUprfootRLZ-8Ou4_ycZLHE3-avcg4mvqGEix8KMvA6gJowXXBOQ8KOsRmwQKgISOElRCCIEMeMCbaPxiCGbOmMBaYAaJpHz122E1T_-6s26pV5YxdLvXa1jun2hwNKWatETqjaWrnGluqTVOtdPOnAKt9j-qkR0WJYqLNPBzgu2JlF8dEV1wrv3byj9vqL3uUddMylvYUCCEXeyh0g4mjyXzrRtk1_QdBgoM_</recordid><startdate>1979</startdate><enddate>1979</enddate><creator>MISUMI, MASAROU</creator><creator>YAMAKI, HIROSHI</creator><creator>AKIYAMA, TETSU</creator><creator>TANAKA, NOBUO</creator><general>JAPAN ANTIBIOTICS RESEARCH ASSOCIATION</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>7X8</scope></search><sort><creationdate>1979</creationdate><title>MECHANISM OF ACTION OF ACLACINOMYCIN A II. THE INTERACTION WITH DNA AND WITH TUBULIN</title><author>MISUMI, MASAROU ; YAMAKI, HIROSHI ; AKIYAMA, TETSU ; TANAKA, NOBUO</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3208-1ff7eab13b6ab6667b350cd471394224f19182567448882c2044ecbce14c12a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1979</creationdate><topic>Antibiotics, Antineoplastic - metabolism</topic><topic>Chemical Phenomena</topic><topic>Chemistry</topic><topic>Dialysis</topic><topic>DNA - metabolism</topic><topic>Glycoproteins - metabolism</topic><topic>Hot Temperature</topic><topic>Naphthacenes - metabolism</topic><topic>Nucleic Acid Denaturation</topic><topic>Polydeoxyribonucleotides - metabolism</topic><topic>Protein Binding</topic><topic>Tubulin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>MISUMI, MASAROU</creatorcontrib><creatorcontrib>YAMAKI, HIROSHI</creatorcontrib><creatorcontrib>AKIYAMA, TETSU</creatorcontrib><creatorcontrib>TANAKA, NOBUO</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><jtitle>Journal of antibiotics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>MISUMI, MASAROU</au><au>YAMAKI, HIROSHI</au><au>AKIYAMA, TETSU</au><au>TANAKA, NOBUO</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>MECHANISM OF ACTION OF ACLACINOMYCIN A II. THE INTERACTION WITH DNA AND WITH TUBULIN</atitle><jtitle>Journal of antibiotics</jtitle><addtitle>J. Antibiot.</addtitle><date>1979</date><risdate>1979</risdate><volume>32</volume><issue>1</issue><spage>48</spage><epage>52</epage><pages>48-52</pages><issn>0021-8820</issn><eissn>1881-1469</eissn><abstract>Aclacinomycin A was observed to effect the thermal denaturation of DNA and to increase Tm. The visible absorption spectrum of the antibiotic showed bathochromic and hypochromic shifts upon reaction with native and heat-denatured DNA. [14C]Aclacinomycin A was demonstrated by equilibrium dialysis to bind to DNA. Native calf thymus DNA appeared to possess one binding site per ca. 6 nucleotides for the antibiotic with an apparent association constant of ca. 1.2×106 M-1. Heat-denatured DNA showed much less affinity for the antibiotic: one binding site per ca. 6 nucleotides with an apparent binding constant of ca. 3.5×104 M-1. The difference of association constants between double- and single-stranded DNAs suggested that the antibiotic may be intercalated between base pairs of the DNA double helix. [14C]Aclacinomycin A exhibited higher affinity for poly(dAdT) than for poly(dIdC). The antibiotic showed a significant difference spectrum with porcine tubulin, indicating an interaction with tubulin. The binding to tubulin was also demonstrated by equilibrium dialysis of [14C]aclacinomycin A and tubulin.</abstract><cop>Japan</cop><pub>JAPAN ANTIBIOTICS RESEARCH ASSOCIATION</pub><pmid>761992</pmid><doi>10.7164/antibiotics.32.48</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0021-8820 |
| ispartof | The Journal of Antibiotics, 1979, Vol.32(1), pp.48-52 |
| issn | 0021-8820 1881-1469 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_74439304 |
| source | J-STAGE Free; MEDLINE |
| subjects | Antibiotics, Antineoplastic - metabolism Chemical Phenomena Chemistry Dialysis DNA - metabolism Glycoproteins - metabolism Hot Temperature Naphthacenes - metabolism Nucleic Acid Denaturation Polydeoxyribonucleotides - metabolism Protein Binding Tubulin - metabolism |
| title | MECHANISM OF ACTION OF ACLACINOMYCIN A II. THE INTERACTION WITH DNA AND WITH TUBULIN |
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