Himeshima T, Hatakeyama T, Yamasaki N
Laboratory of Biochemistry, Faculty of Agriculture, Kyushu University, Fukuoka.
J Biochem. 1994 Apr;115(4):689-92. doi: 10.1093/oxfordjournals.jbchem.a124397.
The complete amino acid sequence of SJL-I, a lectin from the sea cucumber, Stichopus japonicus, was determined by sequence analysis of peptides derived on enzymatic and chemical fragmentation of the protein. SJL-I consists of 143 amino acid residues and its molecular mass was calculated to be 15,837 Da. Comparison of the sequence of SJL-I with a database revealed that SJL-I exhibits apparent homology with C-type lectins, especially with those of marine invertebrates. The highest homology (identity 28.6%) was found with echinoidin, a lectin from the sea urchin, Anthocidaris crassispina. Comparison of the sequence of SJL-I with those of other C-type lectins indicated that the conserved amino acids are relatively abundant in the C-terminal half of their carbohydrate-recognition domains (CRDs), that can be considered to be involved in binding with Ca2+ as well as carbohydrates.
通过对日本刺参中提取的凝集素SJL-I经酶解和化学裂解得到的肽段进行序列分析，确定了其完整的氨基酸序列。SJL-I由143个氨基酸残基组成，计算得到的分子量为15,837道尔顿。将SJL-I的序列与数据库进行比较后发现，SJL-I与C型凝集素具有明显的同源性，尤其是与海洋无脊椎动物的C型凝集素。与来自厚刺海胆的凝集素echinoidin的同源性最高（同一性为28.6%）。将SJL-I的序列与其他C型凝集素的序列进行比较表明，保守氨基酸在其碳水化合物识别结构域（CRD）的C端一半中相对丰富，这些保守氨基酸可被认为参与与Ca2+以及碳水化合物的结合。
