Endo Noriyuki, Nogata Yasuyuki, Yoshimura Erina, Matsumura Kiyotaka
Central Research Institute of Electric Power Industry, Abiko-shi, Chiba-ken, Japan.
Biofouling. 2009;25(5):429-34. doi: 10.1080/08927010902875113.
A previously undescribed larval settlement-inducing protein was purified from adult extracts of the barnacle, Balanus amphitrite (=Amphibalanus amphitrite). Results of SDS-PAGE indicated that the relative molecular mass of the protein in reduced and denatured form is 31,600 +/- 500 kDa, and that it is distinct from the Settlement Inducing Protein Complex (SIPC) which has previously been determined as a larval settlement-inducing pheromone. The N-terminal 33-residue sequence of the intact protein showed no similarity with previously reported proteins in the EMBL/Genbank/DDBJ databases. The purified protein at a concentration of 10 microg ml(-1) induced approximately four times more larval settlement than the control (filtered natural seawater). In addition, results of the assay using both 24-well polystyrene plates and agarose gels indicated that this protein is probably released into seawater and attracts cypris larvae. These results suggest that the purified protein is a waterborne type pheromone which induces settlement of larvae of B. amphitrite.
从藤壶（纹藤壶，即中华哲水蚤）成虫提取物中纯化出一种此前未被描述的诱导幼虫附着的蛋白质。SDS - PAGE结果表明，该蛋白质在还原和变性形式下的相对分子质量为31,600±500 kDa，且与先前被确定为诱导幼虫附着信息素的附着诱导蛋白复合物（SIPC）不同。完整蛋白质的N端33个残基序列与EMBL/Genbank/DDBJ数据库中先前报道的蛋白质没有相似性。浓度为10微克/毫升的纯化蛋白诱导的幼虫附着量比对照（过滤后的天然海水）多约四倍。此外，使用24孔聚苯乙烯板和琼脂糖凝胶进行的测定结果表明，这种蛋白质可能释放到海水中并吸引金星幼虫。这些结果表明，纯化的蛋白质是一种水溶性信息素，可诱导纹藤壶幼虫附着。
