Carcinogen aflatoxin B1 is located preferentially in internucleosomal deoxyribonucleic acid following exposure in vivo in rainbow trout.
Carcinogen aflatoxin B1 is located preferentially in internucleosomal deoxyribonucleic acid following exposure in vivo in rainbow trout.
复制标题
虹鳟鱼体内暴露后，致癌物黄曲霉毒素 B1 优先位于核小体间脱氧核糖核酸中。
DOI：
10.1021/bi00566a027
复制
发表时间：
1980
期刊：
影响因子：
2.9
通讯作者：
VanHolde,KE
中科院分区：
文献类型：
--
作者：
Bailey,GS;Nixon,JE;Hendricks,JD;Sinnhuber,RO;VanHolde,KE
George S. Bailey,* Joseph E. Nixon, Jerry D. Hendricks, Russell O. Sinnhuber, and Kensal E. Van Holde abstract: The purpose of this work was to investigate the distribution in chromatin of deoxyribonucleicacid (DNA) adducts of aflatoxin Bb following exposure in vivo. Rainbow trout were injected intraperitoneally with radiolabeled aflatoxin Bi, a potent procarcinogen known to readily induce hepato-cellular carcinomas in these fish. After maximum incorporation, liver nuclei were prepared and digested with micro--Ajthough chemical carcinogens are believed to initiate their action through mutagenic interaction with the genome (Miller & Miller, 1971; Ames, 1979), our knowledge of the actual sites of carcinogen attack in higher organisms is at present very limited. One initial approach to this problem involves exam-ining the influence of those chromatin structural features which one can clearly define on the accessibility of carcinogens to DNA in vivo. The genome of all eukaryotes is now recognized to be organized into a repeating subunit structure [for reviews, see Kornberg (1977); Garret (1979)]. This structure, called the nucleosome, consists of about 165-245 base pairs of DNA1 together with all of the histones. The nucleosome can in turn be subdivided into a ubiquitous “core particle” containing 146 base pairs of DNA wound one and three-fourths turns around a core of eight histone molecules (two each of histones H2A, H2B, H3, and H4) and a variable region of 20-70 base pairs of “linker” DNA. The linker provides additional binding sites for histones HI and other nonhistone proteins of suspected regulatory or structural function (Noll & Kornberg, 1977; Lohr et al., 1977a; Levy-Wilson et al., 1979; Weisbrod et al., 1980). These elements, perhaps in combination with local
