The covalent protein structure of insecticyanin, a blue biliprotein from the hemolymph of the tobacco hornworm, Manduca sexta L.
The covalent protein structure of insecticyanin, a blue biliprotein from the hemolymph of the tobacco hornworm, Manduca sexta L.
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昆虫青素的共价蛋白质结构，昆虫青素是一种来自烟草天蛾（Manduca sexta L）血淋巴的蓝色胆蛋白。
DOI：
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发表时间：
1984
影响因子：
4.8
通讯作者：
J. H. Law
中科院分区：
文献类型：
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作者：
C. Riley;B. K. Barbeau;P. Keim;F. Kézdy;R. Heinrikson;J. H. Law
测定了烟草天蛾五龄幼虫血淋巴中昆虫花青素的氨基酸序列。脱辅基蛋白是189个氨基酸的单链多肽，分子量21，378，含有两个二硫键，9-119和42-176。通过溴化氰、胰蛋白酶、胰凝乳蛋白酶和金黄色葡萄球菌蛋白酶自动Edman降解还原和羧甲基化的昆虫花青苷和由此产生的片段进行序列分析。大多数肽通过反相高效液相色谱法纯化。本文还报道了一种分离昆虫花青苷的高收率纯化方法和一种测定二硫键的简单方法。
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.