Elsevier

Toxicon

Volume 33, Issue 2, February 1995, Pages 171-178
Toxicon

Letter to the editor
Isolation of a polypeptide from Phoneutria nigriventer spider venom responsible for the increased vascular permeability in rabbit skin

https://doi.org/10.1016/0041-0101(94)00148-2Get rights and content

Abstract

Fractionation of Phoneutria nigriventer venom by Sephadex G-10 followed by ion-exchange chromatography yields a fraction (fraction XIII) which increases microvascular permeability in rabbit skin in vivo by activating the tissue kallikrein-kinin system. One polypeptide (PNV3) with the ability to increase microvascular permeability in the rabbit skin in vivo was isolated from fraction XIII and biochemically characterized. PNV3 has 132 amino acid residues with a calculated mol. wt of 14,475. This polypeptide showed the following N-terminal sequence: AVFAIQDQPC. Amino acid analysis indicated the presence of six disulfide bridges and a high content of Glx (20%). Pairwise comparison of PNV3 amino acid sequence with 27 other spider venom polypeptides and proteins indicated that PNV3 presents high similarity (60–70%) with other toxins (Tx2.1, Tx2.5 and Tx2.6) isolated from P. nigriventer venom.

References (31)

  • M Kamada et al.

    Observation of tissue prokallikrein activation by some serine proteases, arginine esterases in rat submandilar gland

    Biochem. Biophys. Res. Commun.

    (1990)
  • S Marangoni et al.

    Biochemical characterization of a vascular smooth muscle contracting polypeptide purified from Phoneutria nigriventer (armed spider) venom

    Toxicon

    (1993)
  • E.H Reimerdes et al.

    Determination of proteolytic activities on casein substrates

  • L Rezende et al.

    Isolation of neurotoxic peptides from the venom of the “armed spider” Phoneutria nigriventer

    Toxicon

    (1991)
  • H.S Selistre et al.

    Isolation and characterization of a thrombin-like enzyme from the venom of the snake Bothrops insularis (jararaca ilhoa)

    Toxicon

    (1987)

    • Cited by (0)

    View full text
    Copyright © 1995 Published by Elsevier Ltd.