Isolation and characterization of equinatoxins from the sea anemone Actinia equina L.
Equinatoxins were purified from the tentacles and bodies of the sea anemone Actinia equina by the use of acetone precipitation, as well as column chromatographies on Sephadex G-50 and CM-cellulose according to the modified method of Macek and Lebez (1988). The equinatoxins obtained, equinatoxin 1 and 2, were hemolytic glycoproteins with a relative molecular mass of 20000. Equinatoxin 2 was found to be rich in glycine, alanine and valine. The amino acid sequences of equinatoxins 1 and 2 were partially determined. A portion of the N-terminal amino acid sequence of equinatoxin 2 was similar to those of pyruvate kinase and sialidase.
Komatsu
S
S
Department of Molecular Biology, National Institute of Agrobiological Resources, Ibaraki, Japan.
Furukawa
K
K
Abe
K
K
Hirano
H
H
Ueda
M
M
D000595:Amino Acid Sequence; D000818:Animals; D000970:Antineoplastic Agents / Q000737:chemistry* / Q000302:isolation & purification*; D003064:Cnidarian Venoms / Q000737:chemistry* / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D012615:Sea Anemones / Q000737:chemistry*
D000970:Antineoplastic Agents; D003064:Cnidarian Venoms; C012307:equinatoxin