Hatakeyama T, Ohuchi K, Kuroki M, Yamasaki N
Laboratory of Biochemistry, Faculty of Agriculture, Kyushu University, Fukuoka, Japan.
Biosci Biotechnol Biochem. 1995 Jul;59(7):1314-7. doi: 10.1271/bbb.59.1314.
The complete amino acid sequence of a Ca(2+)-dependent lectin, CEL-IV, from the marine invertebrate Cucumaria echinata was analyzed. The established sequence showed that CEL-IV comprises 157 amino acid residues with a molecular mass of 17,098 Da (without disulfide bonds). From comparison with other proteins, CEL-IV was apparently homologous with the C-type lectin family. The identity was relatively high with a sea cucumber (Stichopus japonicus) lectin SJL-I (40.0%) and a sea urchin (Anthocidaris crassispina) lectin echinoidin (32.6%). In CEL-IV, one interchain and two intrachain disulfide bonds were identified. Interestingly, one of the two intrachain disulfide bonds that were highly conserved among the other C-type lectins was missing, suggesting that this might be a characteristic feature of C-type lectins in the Holothuroidea.
对来自海洋无脊椎动物刺参的一种钙依赖性凝集素CEL-IV的完整氨基酸序列进行了分析。确定的序列表明，CEL-IV由157个氨基酸残基组成，分子量为17,098 Da（无二硫键）。通过与其他蛋白质比较，CEL-IV明显与C型凝集素家族同源。与海参（日本刺参）凝集素SJL-I（40.0%）和海胆（厚刺海胆）凝集素海胆素（32.6%）的同源性相对较高。在CEL-IV中，鉴定出一个链间二硫键和两个链内二硫键。有趣的是，在其他C型凝集素中高度保守的两个链内二硫键之一缺失，这表明这可能是海参纲C型凝集素的一个特征。
