Amino Acid Sequence and Molecular Characterization of a D-Galactoside-Specific Lectin Purified from Sea Urchin (Anthocidaris crassispina) Eggs

Yasuhiro Ozeki, Taei Matsui, Masami Suzuki, Koiti Titani

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107 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)2391-2394
Number of pages4
JournalBiochemistry
Volume30
Issue number9
DOIs
Publication statusPublished - 01-03-1991

All Science Journal Classification (ASJC) codes

  • Biochemistry

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