79
Views
8
CrossRef citations to date
0
Altmetric
Research Article

A novel cytotoxic protein, Karatoxin, from the dorsal spines of the redfin velvetfish, Hypodytes rubripinnis

, , , , , , , , & show all
Pages 260-265 | Received 05 Feb 2009, Accepted 11 Mar 2009, Published online: 04 Dec 2009

References

  • Baba O, Sano M. (1987). Diel feeding patterns of the congiopodid fish Hypodytes rubripinnis in Aburatsubo Bay, Japan. Japan J Ichthyol. 34(2): 209–214.
  • Barondes SH. (1984). Soluble lectins. A new class of extracellular proteins. Science. 223(4642): 1259–12641.
  • Barondes SH, Cooper DNW, Gitt MA. (1994). Galectins. Structure and function of a large family of animal lectins. J Biol Chem. 269(33): 20807–20810.
  • Bradford MM. (1976). A rapid sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 72: 248–254.
  • Church JE, Hodgson WC. (2002). The pharmacological activity of fish venoms. Toxicon. 40(8): 1083–1093.
  • Davis BJ. (1964). Disc electrophoresis II. Method and application to human serum proteins. Ann NY Acad Sci. 121: 404–427.
  • Drickamer K. (1988). Two distinct classes of carbohydrate-recognition domains in animal lectins. J Biol Chem. 263(20): 9557–9560.
  • Giga Y, Ikai A, Takahashi K. (1987). The complete amino acid sequence of a lectin from the coelomic fluid of the sea urchin Anthrocidaris crassispina: Homologies with mammalian and insect lectins. J Biol Chem. 262(13): 6197–6203.
  • Hatakeyama T, Nagatomo H, Yamasaki N. (1995). Interaction of the hemolytic lectin CEL-III from the marine invertebrate Cucumaria echinata with the erythrocyte membrane. J Biol Chem. 270(8): 3560–3564.
  • Hosono M, Ishikawa K, Mineki R, Murayama K, Numata C, Ogawa Y, Takayanagi Y, Nitta K. (1999). Tandem repeat structure of rhamnose-binding lectin from catfish (Silurus asotus) eggs. Biochim Biophys Acta. 1472(3): 668–675.
  • Kawagishi H, Yamawaki H, Isobe S, Usui T, Kimura A, Chiba S. (1994). Two lectins from the marine sponge Halichondria okadai. J Biol Chem. 269(2): 1375–1379.
  • Kikuchi T. (1966). An ecological study on animal communities of the Zostera marina belt in Tomioka Bay, Amakusa, Kyushu. Publ Amakusa Mar Biol Lab. 1(1): 1–106.
  • Laemmli UK. (1970). Cleavage of structural protein during the assembly of the head of the bacteriophage T4. Nature. 227(5259): 680–685.
  • Maretic Z. (1988). Fish venoms. In: Tu AT, ed. Handbook of Natural Toxins, Vol. 3. Marine Toxins and Venoms. New York, USA: Marcel Dekker. p. 445–476.
  • Nakagawa N, Yamaguchi C, Yamada H, Nagasaka K, Nagasaka T. (1995). Preliminay study on the venom of scorpionfish, Hypodytes rubripinnis. Comp Physiol Biochem. 12(4): 339.
  • Nakagawa H, Yamaguchi C, Hayashi H. (1997). Biologically active substances from sea urchins. J Natural Toxins. 6(2): 193–202.
  • Nakagawa H, Tanigawa T, Tomita K, Tomihara Y, Araki Y, Tachikawa E. (2003). Recent studies on the pathological effects of purified sea urchin toxins. J Toxicol Toxin Rev. 22(4): 633–649.
  • Russel FE. (1965). Marine toxins and venomous and poisonous marine animals. In: Russel FE. ed. Advances in Marine Biology, Vol. 3. London, UK: Academic Press. p. 255–384.
  • Satoh F, Nakagawa H, Yamada H, Nagasaka K, Nagasaka T, Araki Y, Tomihara Y, Nozaki M, Sakuraba H, Ohshima T, Hatakeyama T, Aoyagi H. (2002). Fishing for bioactive substances from scorpionfish and some sea urchins. J Natural Toxins. 11(4): 297–304.
  • Saunders PR. (1960). Pharmacological and chemical studies of the venom of stonefish (Genus Synanceja) and other scorpionfishes. Ann NY Acad Sci. 90: 789–804.
  • Tange Y. (1954). Morphology of the poison apparatus in Japanese fish with comments on its toxicity. V. Poison apparatus in Hypodytes rubripinnis (Temminck et Schlegel). Yokohama Med Bull. 5(1): 42–48.
  • Ueno K, Kang J-H. (1992). Multiple sex chromosomes in the redfin velvetfish, Hypodytes rubripinnis. Japan J Ichthyol. 39(2): 170–173.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.