Dasgupta D, Rajgopalan R, Gurnani S
FEBS Lett. 1983 Feb 7;152(1):101-4. doi: 10.1016/0014-5793(83)80491-8.
Role of lysine residues in the colchicine binding site and in the assembly-disassembly process was examined. It was observed that at 4 degrees C (pH 7.5-8, 8 +/- 1) lysine residues and the N-terminal methionine residue of tubulin were all buried within the molecule. Evidence indicates that epsilon-amino groups of lysine residues of tubulin are shared by both the colchicine binding site and the polymerisation process.
研究了赖氨酸残基在秋水仙碱结合位点以及组装-拆卸过程中的作用。观察到在4℃（pH 7.5 - 8，8±1）时，微管蛋白的赖氨酸残基和N端甲硫氨酸残基均埋于分子内部。有证据表明，微管蛋白赖氨酸残基的ε-氨基参与秋水仙碱结合位点及聚合过程。
