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与莱氏无胆甾原体相关的细胞质螺旋结构。

Cytoplasmic helical structure associated with Acholeplasma laidlawii.

作者信息

Kessel M, Peleg I, Muhlrad A, Kahane I

出版信息

J Bacteriol. 1981 Aug;147(2):653-9. doi: 10.1128/jb.147.2.653-659.1981.

Abstract

A distinct spiral protein structure was found in three species of Acholeplasma, but was not found in the Mycoplasma species studied. The spirals, which are 14 nm in width and of variable length from 50 to 300 nm, are formed by a helical arrangement of 7-nm subunits. A rosette-like structure 45 nm in diameter also composed of 7-nm subunits was found in close association with the spirals and may be a taut in vivo form of the spiral. The electrophoretic profile in sodium dodecyl sulfate-polyacrylamide gels indicated that the spirals are composed of a predominant polypeptide with an apparent molecular weight of 100,000. No evidence can be found for inferring actin-like properties for this structure.

摘要

在三种无胆甾原体中发现了一种独特的螺旋蛋白结构,但在所研究的支原体物种中未发现。这些螺旋体宽度为14纳米,长度从50到300纳米不等,由7纳米的亚基呈螺旋状排列形成。还发现了一种直径为45纳米、同样由7纳米亚基组成的玫瑰花结样结构,它与螺旋体紧密相连,可能是螺旋体在体内的一种紧密形式。十二烷基硫酸钠-聚丙烯酰胺凝胶电泳图谱表明,螺旋体由一种表观分子量为100,000的主要多肽组成。没有证据可以推断这种结构具有肌动蛋白样特性。

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