The amino acid sequence of Acanthamoeba profilin.
The amino acid sequence of Acanthamoeba profilin.
复制标题
棘阿米巴 profilin 的氨基酸序列。
DOI：
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发表时间：
1985
影响因子：
4.8
通讯作者：
Edward D. Korn
中科院分区：
文献类型：
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作者：
C. Ampe;Joël Vandekerckhove;Stephen L Brenner;L. Tobacman;Edward D. Korn
通过将胰蛋白酶、胰凝乳蛋白酶、嗜热菌蛋白酶和金黄色葡萄球菌V8蛋白酶肽与葡聚糖裂解产物的部分NH 2-末端序列比对，确定了阿米巴profilin的完整氨基酸序列。阿米巴profilin含有125个氨基酸残基，是NH 2-末端封闭的，并在位置103处具有三甲基赖氨酸。在序列中的5个位置处，鉴定了两个氨基酸，表明变形虫表达至少两种略微不同的profilins。带电残基分布不均匀，NH 2-末端的一半非常疏水，COOH-末端的一半特别富含碱性残基。阿米巴profilin序列与小牛脾profilin序列的比较（Nystrom，L. E、林德伯格，美国，Kendrick-Jones，J.，和Jakes，R. 04 The Dog of the Woman（1979）101，161-165）揭示了NH 2-末端区域的同源性。因此，我们认为，该区域参与肌动蛋白结合活性。
The complete amino acid sequence of Acanthamoeba profilin was determined by aligning tryptic, chymotryptic, thermolysin, and Staphylococcus aureus V8 protease peptides together with the partial NH2-terminal sequences of the tryptophan-cleavage products. Acanthamoeba profilin contains 125 amino acid residues, is NH2-terminally blocked, and has trimethyllysine at position 103. At five positions in the sequence two amino acids were identified indicating that the amoebae express at least two slightly different profilins. Charged residues are unevenly distributed, the NH2-terminal half being very hydrophobic and the COOH-terminal half being especially rich in basic residues. Comparison of the Acanthamoeba profilin sequence with that of calf spleen profilin (Nystrom, L. E., Lindberg, U., Kendrick-Jones, J., and Jakes, R. (1979) FEBS Lett. 101, 161-165) reveals homology in the NH2-terminal region. We suggest, therefore, that this region participates in the actin-binding activity.