<?xml version="1.0" encoding="utf-8"?>
<journal>
<title>Medical Journal of the Islamic Republic Of Iran</title>
<title_fa>مجله پزشکی جمهوری اسلامی ایران</title_fa>
<short_title>Med J Islam Repub Iran</short_title>
<subject>Medical Sciences</subject>
<web_url>http://mjiri.iums.ac.ir</web_url>
<journal_hbi_system_id>2</journal_hbi_system_id>
<journal_hbi_system_user>journal2</journal_hbi_system_user>
<journal_id_issn>1016-1430</journal_id_issn>
<journal_id_issn_online>2251-6840</journal_id_issn_online>
<journal_id_pii>8</journal_id_pii>
<journal_id_doi>10.18869/mjiri</journal_id_doi>
<journal_id_iranmedex></journal_id_iranmedex>
<journal_id_magiran></journal_id_magiran>
<journal_id_sid>14</journal_id_sid>
<journal_id_nlai>8888</journal_id_nlai>
<journal_id_science>13</journal_id_science>
<language>en</language>
<pubdate>
	<type>jalali</type>
	<year>1371</year>
	<month>11</month>
	<day>1</day>
</pubdate>
<pubdate>
	<type>gregorian</type>
	<year>1993</year>
	<month>2</month>
	<day>1</day>
</pubdate>
<volume>6</volume>
<number>4</number>
<publish_type>online</publish_type>
<publish_edition>1</publish_edition>
<article_type>fulltext</article_type>
<articleset>
	<article>


	<language>en</language>
	<article_id_doi></article_id_doi>
	<title_fa></title_fa>
	<title>BINDING OF THE ANTITUMOR DRUG ADRIAMYCIN TO DNA-HISTONE COMPLEXES</title>
	<subject_fa>Biological Sciences</subject_fa>
	<subject>Biological Sciences</subject>
	<content_type_fa>Original Research: Basic Science in Medicine</content_type_fa>
	<content_type>Original Research: Basic Science in Medicine</content_type>
	<abstract_fa></abstract_fa>
	<abstract>Isotherms of the binding of the anthracycIine antibiotic, adriamycin
(adriblastin), to DNA histone complexes was studied by means of spectroscopic
analysis. The results indicated that: (a) binding of adriamycin to histones
reduced the interaction of histones with DNA, (b) binding of the drug to DNA
did not change the binding affinity of histone to DNA and, (c) in the explored
binding range of r&lt;O.1 the binding of adriamycin to DNA-histone complex
proved to be anticooperative with n values of 0.32 for the interaction of histone
with DNA-drug and 0.26 for the binding of DNA to histone-drug complex. The
results suggest the possible participation of his tones in the DNA-drug complex
formation.
</abstract>
	<keyword_fa></keyword_fa>
	<keyword>Anthracycline, Chromation, Histones, Adriomycin</keyword>
	<start_page>275</start_page>
	<end_page>279</end_page>
	<web_url>http://mjiri.iums.ac.ir/browse.php?a_code=A-10-298-674&amp;slc_lang=en&amp;sid=1</web_url>


<author_list>
	<author>
	<first_name>AZRA</first_name>
	<middle_name></middle_name>
	<last_name>RABBANI</last_name>
	<suffix></suffix>
	<first_name_fa></first_name_fa>
	<middle_name_fa></middle_name_fa>
	<last_name_fa></last_name_fa>
	<suffix_fa></suffix_fa>
	<email></email>
	<code>20031947532846006259</code>
	<orcid>20031947532846006259</orcid>
	<coreauthor>Yes
</coreauthor>
	<affiliation>From the Institute of Biochemistry and Biophysics, Tehran University of Medical Sciences, Tehran, Islamic Republic of Iran.</affiliation>
	<affiliation_fa></affiliation_fa>
	 </author>


	<author>
	<first_name>MARZIEH</first_name>
	<middle_name></middle_name>
	<last_name>HAGSHARIFIA TAGAVI</last_name>
	<suffix></suffix>
	<first_name_fa></first_name_fa>
	<middle_name_fa></middle_name_fa>
	<last_name_fa></last_name_fa>
	<suffix_fa></suffix_fa>
	<email></email>
	<code>20031947532846006260</code>
	<orcid>20031947532846006260</orcid>
	<coreauthor>No</coreauthor>
	<affiliation></affiliation>
	<affiliation_fa></affiliation_fa>
	 </author>


	<author>
	<first_name>BAHRAM</first_name>
	<middle_name></middle_name>
	<last_name>GOLIAEI</last_name>
	<suffix></suffix>
	<first_name_fa></first_name_fa>
	<middle_name_fa></middle_name_fa>
	<last_name_fa></last_name_fa>
	<suffix_fa></suffix_fa>
	<email></email>
	<code>20031947532846006261</code>
	<orcid>20031947532846006261</orcid>
	<coreauthor>No</coreauthor>
	<affiliation></affiliation>
	<affiliation_fa></affiliation_fa>
	 </author>


</author_list>


	</article>
</articleset>
</journal>
