Riley C T, Barbeau B K, Keim P S, Kézdy F J, Heinrikson R L, Law J H
J Biol Chem. 1984 Nov 10;259(21):13159-65.
The amino acid sequence has been determined for the insecticyanin from the hemolymph of the fifth instar larvae of the tobacco hornworm, Manduca sexta. The apoprotein is a single polypeptide chain of 189 amino acids, molecular weight 21,378, containing two disulfide bridges, 9-119 and 42-176. The sequence analysis was performed by automated Edman degradation of reduced and carboxymethylated insecticyanin and fragments generated therefrom by cyanogen bromide, trypsin, chymotrypsin, and Staphylococcus aureus proteinase. Most of the peptides were purified by reverse-phase high-performance liquid chromatography. A purification procedure for the isolation of insecticyanin in high yields and a simple method of determining disulfide linkages are also reported.
已经确定了烟草天蛾（Manduca sexta）五龄幼虫血淋巴中昆虫青素的氨基酸序列。脱辅基蛋白是一条由189个氨基酸组成的单多肽链，分子量为21,378，含有两个二硫键，分别位于9-119和42-176位。序列分析是通过对还原和羧甲基化的昆虫青素及其经溴化氰、胰蛋白酶、糜蛋白酶和金黄色葡萄球菌蛋白酶产生的片段进行自动Edman降解来进行的。大多数肽通过反相高效液相色谱法纯化。还报道了一种高产率分离昆虫青素的纯化方法和一种确定二硫键连接的简单方法。
