- 著者
-
Hatakeyama Tomomitsu
Himeshima Tomoharu
Komatsu Akane
Yamasaki Nobuyuki
- 出版者
- 社団法人日本農芸化学会
- 雑誌
- Bioscience, Biotechnology, and Biochemistry (ISSN:09168451)
- 巻号頁・発行日
- vol.57, no.10, pp.1736-1739, 1993-10-23
- 被引用文献数
-
2
15
Two Ca^<2+>-dependent lectins were purified from the sea cucumber Stichopus japonicus by affinity chromatography on lactosyl-Sepharose 4B and ion-exchange chromatography on Q-Sepharose. Their molecular masses were estimated to be 13 kDa (SJL-I) and 15 kDa (SJL-II) on SDS-PAGE. SJL-I agglutinated rabbit erythrocytes as well as human A, B, and O-type erythrocytes, but SJL-II agglutinated only rabbit erythrocytes. Hemagglutination by SJL-I was competitively inhibited by N-acetyl-D-galactosamine and galactose-containing carbohydrates. On the other hand, only lactose, melibiose, and raffinose gave weak inhibition of hemagglutination by SJL-II, suggesting that SJL-II may have high specificity for particular complex carbohydrate(s) on the surface of rabbit erythrocytes. SJL-II was activated at ten times lower Ca^<2+> concentration than SJL-I. Both lectins lost activity in acidic pH, while SJL-I appeared more stable down to pH 4.5.