| Resistance of H1 histone to proteolytic attack in chromatin from rat-ascites hepatoma. | |
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MedLine Citation:
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PMID: 6360339 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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From rat-liver and ascites-hepatoma chromatins, NaCl-soluble fractions were prepared. The 0.35 M NaCl-soluble fraction from the hepatoma (AH) chromatin contained much non-histone protein of high-molecular weight, compared with the fraction from the rat-liver (RL) chromatin. The 0.35 M NaCl-insoluble, but 2 M NaCl/5 M urea-soluble fraction was composed mainly of 5 classes of histones. These histones were quantitatively not different between AH and RL chromatins. However, H1 histone was rather protease-resistant in AH chromatin, but not in RL chromatin. The proteolytic capacity was also lower in AH chromatin. In addition, in the micrococcal-nuclease digest of AH nuclei, the oligonucleosomes were considerably retained even by long-time digestion, but not in that of RL nuclei. |
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Authors:
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K Kishida; N Sugano |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Cancer letters Volume: 21 ISSN: 0304-3835 ISO Abbreviation: Cancer Lett. Publication Date: 1983 Dec |
Date Detail:
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Created Date: 1984-02-23 Completed Date: 1984-02-23 Revised Date: 2004-11-17 |
Medline Journal Info:
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Nlm Unique ID: 7600053 Medline TA: Cancer Lett Country: NETHERLANDS |
Other Details:
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Languages: eng Pagination: 125-31 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Chromatin / enzymology*, isolation & purification Electrophoresis, Polyacrylamide Gel Histones / metabolism* Liver / ultrastructure Liver Neoplasms, Experimental / ultrastructure* Male Micrococcal Nuclease / metabolism Peptide Hydrolases / metabolism* Rats |
| Chemical | |
Reg. No./Substance:
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0/Chromatin; 0/Histones; EC 3.1.31.1/Micrococcal Nuclease; EC 3.4.-/Peptide Hydrolases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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