Schneider H J, Drexel R, Feldmaier G, Linzen B, Lottspeich F, Henschen A
Hoppe Seylers Z Physiol Chem. 1983 Oct;364(10):1357-81. doi: 10.1515/bchm2.1983.364.2.1357.
The complete amino-acid sequence of subunit e of the hemocyanin from the tarantula, Eurypelma californicum, was determined by a combination of manual and automated methods. By limited proteolysis with chymotrypsin, two large fragments (e-CHn 29 and e-CHn 42) were obtained. The large peptides were further cleaved with cyanogen bromide, trypsin (with and without prior blocking of lysine residues), chymotrypsin, Staphylococcus aureus proteinase, Astacus fluviatilis proteinase, or 25% formic acid. The complete chain comprises 621 residues. A remarkable feature of the sequence is a hexapeptide -His-His-Trp-His-Trp-His- which is believed to take part in the binding of copper.
通过手工和自动化方法相结合,测定了捕鸟蛛(Eurypelma californicum)血蓝蛋白亚基e的完整氨基酸序列。用胰凝乳蛋白酶进行有限的蛋白水解,得到了两个大片段(e-CHn 29和e-CHn 42)。这些大肽段再用溴化氰、胰蛋白酶(赖氨酸残基有无预先封闭)、胰凝乳蛋白酶、金黄色葡萄球菌蛋白酶、螯虾蛋白酶或25%甲酸进一步裂解。完整的链由621个残基组成。该序列的一个显著特征是一个六肽——-His-His-Trp-His-Trp-His-,据信它参与铜的结合。