Lu R C, Elzinga M
Biochim Biophys Acta. 1978 Dec 20;537(2):320-8. doi: 10.1016/0005-2795(78)90515-9.
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.
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。