title: Amino acid sequence studies on cytolytic toxins from sea anemone Heteractis magnifica, Entacmaea quadricolor and Stichodactyla mertensii (Anthozoa).
abstract: The complete amino acid sequence of a cytolytic toxin, HmT, isolated from sea anemone Heteractis magnifica was determined. It is composed of 177 amino acid residues and lacks half-cystines. Partial N-terminal sequences of three other cytolysins from Entacmaea quadricolor (EnT) and Stichodactyla mertensii (SmT-1 and SmT-2) were also determined. Comparing these sequences with those of other sea anemone cytolysins, a high degree of homology was observed.
authors.affiliation: The Institute of Medicinal Chemistry, Hoshi University, Shinagavwa, Tokyo, Japan. samejima@hoshi.ac.jp
authors.forename: Y
authors.initials: Y
authors.lastname: Samejima
authors.forename: M
authors.initials: M
authors.lastname: Yanagisawa
authors.forename: Y
authors.initials: Y
authors.lastname: Aoki-Tomomatsu
authors.forename: E
authors.initials: E
authors.lastname: Iwasaki
authors.forename: J
authors.initials: J
authors.lastname: Ando
authors.forename: D
authors.initials: D
authors.lastname: Mebs
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D003603:Cytotoxins / Q000737:chemistry*; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D012615:Sea Anemones; D017386:Sequence Homology, Amino Acid
chemical_list: D003603:Cytotoxins