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嗜热四膜虫纤毛动力蛋白与外纤维的重组。

Recombination of ciliary dynein of Tetrahymena with the outer fibers.

作者信息

Shimizu T

出版信息

J Biochem. 1975 Jul;78(1):41-9.

PMID:378
Abstract

Recombination of ciliary dyneins of Tetrahymena pyriformis with the outer fibers was investigated using turbidimetry, co-sedimentation analysis and electron microscopy. As reported by Gibbons, 30S dynein could recombine with the outer fibers, while 14S dynein did to so a lesser extent. At acidic pH, however, most of the 14S dynein was also rebound to the outer fibers. When an excess of crude dynein fraction was added to the outer fiber fraction at pH 8.2, electron microscopic observations showed that the outer doublet microtubules were decorated not only with arms but also with other electron-dense materials. On the other hand, when crude dynein fraction was mixed with the outer fibers in an appropriate quantity, only arms were reconstituted at the regular positions of A-subfibers. ATP had an inhibitory effect on the recombination of dynein with the outer fibers.

摘要

利用比浊法、共沉降分析和电子显微镜研究了梨形四膜虫纤毛动力蛋白与外纤维的重组。如吉本斯所报道,30S动力蛋白能与外纤维重组,而14S动力蛋白的重组程度较小。然而,在酸性pH条件下,大部分14S动力蛋白也能与外纤维重新结合。当在pH 8.2时向外纤维组分中加入过量的粗动力蛋白组分时,电子显微镜观察显示,外双微管不仅被臂装饰,还被其他电子致密物质装饰。另一方面,当粗动力蛋白组分与外纤维以适当数量混合时,仅在A亚纤维的规则位置重建了臂。ATP对动力蛋白与外纤维的重组有抑制作用。

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