Studies on the subunit structure of textilotoxin, a potent presynaptic neurotoxin from the venom of the Australian common brown snake (Pseudonaja textilis). 3. The complete amino-acid sequences of all the subunits.

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  • Author(s): Pearson JA;Pearson JA; Tyler MI; Retson KV; Howden ME
  • Source:
    Biochimica et biophysica acta [Biochim Biophys Acta] 1993 Feb 13; Vol. 1161 (2-3), pp. 223-9.
  • Publication Type:
    Journal Article; Research Support, Non-U.S. Gov't
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Elsevier Pub. Co Country of Publication: Netherlands NLM ID: 0217513 Publication Model: Print Cited Medium: Print ISSN: 0006-3002 (Print) Linking ISSN: 00063002 NLM ISO Abbreviation: Biochim Biophys Acta Subsets: MEDLINE
    • Publication Information:
      Original Publication: Amsterdam : Elsevier Pub. Co.
    • Subject Terms:
    • Abstract:
      The complete amino-acid sequences of subunits A, B, C and D of textilotoxin, the presynaptic neurotoxin from the venom of the Australian common brown snake, Pseudonaja textilis, were determined. These confirmed that it is structurally the most complex of any of the known snake venom neurotoxins. Textilotoxin consists of 623 amino-acid residues in five subunits (subunit A, 118 residues; subunit B, 121 residues; subunit C, 118 residues; subunit D, two chains of 133 residues each). All subunits A, B, C and D contain the putative phospholipase A2 active site. Only subunit A showed any lethality on its own (4 mg/kg i.v. in mice). Subunit D contained two identical covalently-linked subunits and was weakly glycosylated. All subunits were necessary for maximum lethality at 1 micrograms/kg mice intraperitoneally. Details of the sequences of the subunits A, B and C are reported and interesting homology with other snake venom phospholipase A2 neurotoxins indicated.
    • Accession Number:
      0 (Elapid Venoms)
      0 (Neurotoxins)
      85666-96-2 (textilotoxin)
    • Publication Date:
      Date Created: 19930213 Date Completed: 19930316 Latest Revision: 20190610
    • Publication Date:
      20240829
    • Accession Number:
      10.1016/0167-4838(93)90217-f
    • Accession Number:
      8431471