Isolation and partial characterization of a L-rhamnose-binding lectin from the globiferous pedicellariae of the toxopneustid sea urchin, Toxopneustes pileolus

Authors

• Hitomi Sakai ¹
• Kozue Edo ^{1, 2}
• Hideyuki Nakagawa ¹
• Mitsuko Shinohara ³
• Rie Nishiitsutsuji ³
• Kiyoshi Ohura ³

¹ Division of Environmental Symbiosis, Graduate School of Integrated Arts and Sciences, The University of Tokushima, Tokushima 770-8502, Japan

² Department of Science for Human Health, Junior College Division, Shikoku University, Tokushima 771-1192, Japan.

³ Department of Pharmacology, Osaka Dental University, Hirakata 573-1121, Japan.

10.1186/2008-6970-5-12

Abstract

A novel lectin from the large globiferous pedicellariae of the toxopneustid sea urchin, Toxopneustes pileolus, was isolated by a combination of gel permeation chromatography and affinity chromatography techniques. On an SDS-PAGE gel, single bands were detected with relative molecular weights of 28 and 170 kDa in the presence and absence of 2-mercaptoethanol, respectively, suggesting that this lectin is present as a homohexamer. The 170-kDa lectin was named sea urchin lectin-III (SUL-III). The N-terminal partial amino acid sequence of the intact 28-kDa subunit of SUL-III was determined as follows: RCPQPAALPYRIAQIGNRFL. Agglutination of rabbit erythrocytes by SUL-III was most effectively inhibited by L-rhamnose. SUL-III induced mitogenic stimulation on murine splenocytes. These results suggest that SUL-III may be a novel L-rhamnose-binding lectin with potent bioactivity.

Keywords

• : Sea urchin
• Toxopneustes pileolus
• L-rhamnose-binding lectin
• Rabbit erythrocytes
• Agglutination
• Mitogenic activity
• Murine splenocytes

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