- 著者
- Tomoharu Himeshima Tomomitsu Hatakeyama Nobuyuki Yamasaki
- 出版者
- The Japanese Biochemical Society
- 雑誌
- The Journal of Biochemistry (ISSN:0021924X)
- 巻号頁・発行日
- vol.115, no.4, pp.689-692, 1994-04-01 (Released:2008-11-18)
- 参考文献数
- 21
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.