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从多头绒泡菌细胞核中分离出一种残留蛋白质结构。

Isolation of a residual protein structure from nuclei of the myxomycete Physarum polycephalum.

作者信息

Mitchelson K R, Bekers A G, Wanka F

出版信息

J Cell Sci. 1979 Oct;39:247-56. doi: 10.1242/jcs.39.1.247.

Abstract

A nuclear framework structure has been obtained from isolated interphase nuclei of Physarum polycephalum by extraction with 2.5 M NaCl and subsequent digestion with DNase. Whole-mount electron micrographs showed a nuclear lamina containing residual pore structures associated with the fibrous internal matrix. The matrix was continuous with fibrillar remnants of the nucleolus. The structure was shown to consist of 2 major polypeptides of 23,000 and 36,500 Daltons as well as 30 to 40 minor polypeptides of various molecular weight classes. The 2 major polypeptides were also prominent in preparations of the residual nucleolar material, suggesting that matrix proteins are common to both structures. The predominance of low-molecular-weight polypeptides in Physarum nuclear matrix suggests that there may be significant differences in composition of nuclear structural proteins between lower and higher eukaryotes.

摘要

通过用2.5M氯化钠提取并随后用DNA酶消化,从多头绒泡菌的分离间期核中获得了一种核框架结构。整装电子显微镜照片显示,核纤层含有与纤维状内部基质相关的残余孔结构。基质与核仁的纤维状残余物相连。该结构由23,000和36,500道尔顿的2种主要多肽以及30至40种不同分子量类别的次要多肽组成。这2种主要多肽在残余核仁物质的制备中也很突出,表明基质蛋白是这两种结构共有的。多头绒泡菌核基质中低分子量多肽的优势表明,低等和高等真核生物之间核结构蛋白的组成可能存在显著差异。

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