Takagi T, Konishi K, Mabuchi I
Biological Institute, Faculty of Science, Tohoku University, Sendai, Japan.
J Biol Chem. 1988 Mar 5;263(7):3097-102.
The amino acid sequence of starfish oocyte depactin was determined by aligning lysyl endopeptidase, Staphylococcus aureus V8 protease, and cyanongen bromide peptides. Starfish oocyte depactin is composed of 150 amino acid residues and the N terminus is free proline. The molecular weight is calculated to be 17,590, in good agreement with the value estimated by sodium dodecyl-polyacrylamide gel electrophoresis. Prediction of the secondary structure shows that depactin contains 64% alpha-helix. Comparison of depactin sequence with those of other proteins shows no significant similarity.
通过比对赖氨酰内肽酶、金黄色葡萄球菌V8蛋白酶和溴化氰肽段，确定了海星卵母细胞去肌动蛋白的氨基酸序列。海星卵母细胞去肌动蛋白由150个氨基酸残基组成，N端为游离脯氨酸。计算得到的分子量为17,590，与十二烷基聚丙烯酰胺凝胶电泳估算的值高度一致。二级结构预测表明，去肌动蛋白含有64%的α-螺旋。去肌动蛋白序列与其他蛋白质序列的比较显示无显著相似性。
