Isolation of a novel lectin from the globiferous pedicellariae of the sea urchin Toxopneustes pileolus.
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.
Nakagawa
H
H
Department of Life Science, University of Tokushima, Japan.
Hashimoto
T
T
Hayashi
H
H
Shinohara
M
M
Ohura
K
K
Tachikawa
E
E
Kashimoto
T
T
D000818:Animals; D037102:Lectins / Q000737:chemistry / Q000302:isolation & purification*; D012617:Sea Urchins / Q000737:chemistry*
D037102:Lectins