Artigo Revisado por pares

Amino acid sequence studies on cytolytic toxins from sea anemone Heteractis magnifica, Entacmaea quadricolor and Stichodactyla mertensii (Anthozoa)

2000; Elsevier BV; Volume: 38; Issue: 2 Linguagem: Inglês

10.1016/s0041-0101(99)00154-3

ISSN

1879-3150

Autores

Yuji Samejima, Maho Yanagisawa, Y. Aoki-Tomomatsu, Eyu IWASAKI, Junichi Ando, Dietrich Mebs,

Tópico(s)

Marine Sponges and Natural Products

Resumo

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.

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