title: Amino acid sequence and molecular characterization of a D-galactoside-specific lectin purified from sea urchin (Anthocidaris crassispina) eggs.
abstract: The complete amino acid sequence of a 11.5-kDa subunit of D-galactoside binding lectin purified from sea urchin (Anthocidaris crassispina) eggs is presented. The 105-residue sequence of the subunit was determined by analysis of the intact S-carbamoylmethylated protein and peptides generated by digestion with Achromobacter protease I or Staphylococcus aureus V8 protease. The lectin exists as a disulfide-linked homodimer of two subunits; the dimeric form is essential for hemagglutination activity. However, the monomeric form obtained by partial reduction retains the carbohydrate binding capacity. Neither Ca2+ nor SH reagent is essential for hemagglutination or carbohydrate binding. The sequence has no similarity to that of any known protein and apparently represents a new type of galactoside binding lectin.
authors.affiliation: Division of Biomedical Polymer Science, School of Medicine, Fujita Health University, Aichi, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Ozeki
authors.forename: T
authors.initials: T
authors.lastname: Matsui
authors.forename: M
authors.initials: M
authors.lastname: Suzuki
authors.forename: K
authors.initials: K
authors.lastname: Titani
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D010450:Endopeptidases; D005697:Galactosides / Q000378:metabolism; D037161:Galectins; D006386:Hemagglutination Tests; D006388:Hemagglutinins / Q000737:chemistry* / Q000302:isolation & purification; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D010063:Ovum / Q000737:chemistry; D010446:Peptide Fragments / Q000302:isolation & purification; D011487:Protein Conformation; D011817:Rabbits; D012617:Sea Urchins
chemical_list: D005697:Galactosides; D037161:Galectins; D006388:Hemagglutinins; D046911:Macromolecular Substances; D010446:Peptide Fragments; D010450:Endopeptidases