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微管蛋白的一级结构。α链羧基末端及其他七个溴化氰肽段的序列。

The primary structure of tubulin. Sequences of the carboxyl terminus and seven other cyanogen bromide peptides from the alpha-chain.

作者信息

Lu R C, Elzinga M

出版信息

Biochim Biophys Acta. 1978 Dec 20;537(2):320-8. doi: 10.1016/0005-2795(78)90515-9.

Abstract

The alpha-chain of calf brain tubulin was fragmented by treatment with cyanogen bromide and eight peptides together accounting for 108 residues were purified and sequenced. The COOH-terminal peptide contains a fractional amount (about 0.3 residues) of tyrosine at its COOH-terminus; this presumably represents tyrosine that is added post-translationally to alpha-tubulin. The beta-chain can be phosphorylated, and the probable site of this modification is identified also in the COOH-terminal peptide. Comparison of the sequences described here with the sequence of actin reveals no homology between actin and tubulin.

摘要

用溴化氰处理小牛脑微管蛋白的α链,得到了8个肽段,共108个残基,经纯化后进行了测序。羧基末端肽段在其羧基末端含有少量(约0.3个残基)的酪氨酸;这可能代表翻译后添加到α-微管蛋白上的酪氨酸。β链可以被磷酸化,这种修饰的可能位点也在羧基末端肽段中被确定。将此处描述的序列与肌动蛋白的序列进行比较,发现肌动蛋白和微管蛋白之间没有同源性。

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