Isolation of a novel lectin from the globiferous pedicellariae of the sea urchin Toxopneustes pileolus

H Nakagawa; T Hashimoto; H Hayashi; M Shinohara; K Ohura; E Tachikawa; T Kashimoto

doi:10.1007/978-1-4613-0361-9_14

Isolation of a novel lectin from the globiferous pedicellariae of the sea urchin Toxopneustes pileolus

Adv Exp Med Biol. 1996:391:213-23. doi: 10.1007/978-1-4613-0361-9_14.

Authors

H Nakagawa¹, T Hashimoto, H Hayashi, M Shinohara, K Ohura, E Tachikawa, T Kashimoto

Affiliation

¹ Department of Life Science, University of Tokushima, Japan.

PMID: 8726059
DOI: 10.1007/978-1-4613-0361-9_14

Abstract

Sea urchin lectin-I (SUL-I), a 32 kDa lectin was purified from the large globiferous pedicellariae of the sea urchin, Toxopneustes pileolus by using gel permeation chromatography, ion-exchange chromatography and reverse-phase HPLC. SDS-PAGE showed that SUL-I is a monomeric protein with a molecular mass of 32 kDa. Amino acid analysis indicates SUL-I to contain 294 residues. SUL-I was shown to have chemotactic properties for guinea-pig neutrophils at concentrations of 0.625 microgram/ml. These data suggest that a 32 kDa lectin from T. pileolus may be related to defensive role.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Animals
Lectins / chemistry
Lectins / isolation & purification*
Sea Urchins / chemistry*

Substances

Lectins