Amino acid sequence studies on cytolytic toxins from sea anemone Heteractis magnifica, Entacmaea quadricolor and Stichodactyla mertensii (Anthozoa).
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.
Samejima
Y
Y
The Institute of Medicinal Chemistry, Hoshi University, Shinagavwa, Tokyo, Japan. samejima@hoshi.ac.jp
Yanagisawa
M
M
Aoki-Tomomatsu
Y
Y
Iwasaki
E
E
Ando
J
J
Mebs
D
D
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
D003603:Cytotoxins