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Echinobase
ECB-ART-36390
Adv Exp Med Biol 1996 Jan 01;391:213-23. doi: 10.1007/978-1-4613-0361-9_14.
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Isolation of a novel lectin from the globiferous pedicellariae of the sea urchin Toxopneustes pileolus.

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


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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.

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Genes referenced: LOC100887844 LOC115925415 LOC594261