Purification and characterization of Taiwan cobra venom proteins with weak toxicity

Toxicon. 2005 Jan;45(1):21-5. doi: 10.1016/j.toxicon.2004.09.002.

Abstract

Two proteins G2a and G2b with molecular masses of approximately 24 kDa were isolated from Naja naja atra (Taiwan cobra) venom using sequential chromatography on gel filtration, ion-exchanger and reverse phase columns. The results of Edman degradation and mass analysis revealed that G2a is a cysteine-rich protein reported previously, and G2b is a novel polypeptide. CD spectra showed that the gross conformation of G2a and G2b notably differed. G2a exhibited an activity higher than that noted with G2b on inhibiting carbachol-induced muscle contraction. However, the two proteins weakly blocked muscle contraction evoked by K+. The observations that the two proteins exhibit the toxic activity in the concentration of micromolar range suggest that they are inherently weak toxins as other snake venom cysteine-rich proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bungarotoxins / pharmacology
  • Chickens
  • Circular Dichroism
  • Elapid Venoms / chemistry*
  • Elapid Venoms / toxicity*
  • In Vitro Techniques
  • Muscle Contraction / drug effects
  • Muscle, Skeletal / drug effects
  • Proteins / chemistry
  • Proteins / isolation & purification*
  • Proteins / toxicity

Substances

  • Bungarotoxins
  • Elapid Venoms
  • Proteins