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组蛋白氨基反应特性的研究:游离组蛋白和染色质中组蛋白的反应活性与离子强度的关系。

Studies on the reactive properties of histone amino groups: reactivities of free histones and histones in chromatin as a function of ionic strength.

作者信息

Malchy B L

出版信息

Biochemistry. 1977 Aug 23;16(17):3922-7. doi: 10.1021/bi00636a031.

DOI:10.1021/bi00636a031
PMID:20134
Abstract

The reactivity of the amino groups of the five histones towards acetic anhydride has been measured and with the exception of histone IIb2 the reactivities are very similar to those of exposed lysines with an average pK of 9.5. In addition the reactivities of these groups from 0.20 to 1.0 M NaCl and the reactivity of a peptide containing lysines 5, 8, 12 and 16 of histone IV have been measured in chromatin. It is concluded that at the lower ionic strengths the large proportion of the amino groups are buried for both the histones and the region of histone IV studied. Data obtained from the measurement of the reactivity of standard proline compounds and from a pH and ionic strength study indicate that the N-terminal proline of histone IIb2 is exposed.

摘要

已对五种组蛋白的氨基与乙酸酐的反应活性进行了测定,除组蛋白IIb2外,其他组蛋白的反应活性与平均pK为9.5的暴露赖氨酸的反应活性非常相似。此外,还测定了这些基团在0.20至1.0 M氯化钠中的反应活性以及染色质中含有组蛋白IV的赖氨酸5、8、12和16的肽的反应活性。得出的结论是,在较低离子强度下,所研究的组蛋白和组蛋白IV区域中的大部分氨基都被掩埋。从标准脯氨酸化合物反应活性的测量以及pH和离子强度研究获得的数据表明,组蛋白IIb2的N端脯氨酸是暴露的。

相似文献

1
Studies on the reactive properties of histone amino groups: reactivities of free histones and histones in chromatin as a function of ionic strength.组蛋白氨基反应特性的研究:游离组蛋白和染色质中组蛋白的反应活性与离子强度的关系。
Biochemistry. 1977 Aug 23;16(17):3922-7. doi: 10.1021/bi00636a031.
2
Unmasking of histone amino groups in chromatin at high pH.在高pH值下染色质中组蛋白氨基的暴露
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Complete displacement of somatic histones during transformation of spermatid chromatin: a model experiment.精子细胞染色质转化过程中体细胞组蛋白的完全置换:一项模型实验。
Biochemistry. 1976 May 18;15(10):2047-53. doi: 10.1021/bi00655a004.
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Modification of histone binding in calf thymus chromatin and in the chromatin-protamine complex by acetic anhydride.用乙酸酐对小牛胸腺染色质及染色质-鱼精蛋白复合物中组蛋白结合的修饰作用。
Biochemistry. 1976 May 18;15(10):2041-6. doi: 10.1021/bi00655a003.
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[Unfolding of nucleosome cores induced by chemical acetylation of histones].[组蛋白化学乙酰化诱导核小体核心解折叠]
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Quantitative assessment of chemical artefacts produced by propionylation of histones prior to mass spectrometry analysis.质谱分析前组蛋白丙酰化产生的化学假象的定量评估。
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引用本文的文献

1
Cross-linking of nucleosomal histones with monofunctional imidoesters.核小体组蛋白与单功能亚胺酯的交联
Nucleic Acids Res. 1978 Jul;5(7):2345-58. doi: 10.1093/nar/5.7.2345.