TY - JOUR
T1 - Isolation and characterization of the main toxic fraction from the venom of the false horned viper (Pseudocerastes fieldi)
AU - Batzri-Izraeli, R.
AU - Bdolah, A.
N1 - Funding Information:
Acknowledgements-We thank Prof. E. Kocxvwforvaluable discussion ofthe manuscript and Mra. S. Krnwatorvfor assistance . This work was supported by the Israel Commision for Basic Research .
PY - 1982
Y1 - 1982
N2 - R. Batzri-Izraeli and A. Bdolah. Isolation and characterization of the main toxic fraction from the venom of the false horned viper (Pseudocerastes fieldi). Toxicon 20, 867-875, 1982-The venom of Pseudocerastes fieldi was subjected to gel filtration on Sephadex G-75. Most of the protein and lethality of the venom were eluted in a major symmetrical peak (C). The lethality of this peak is confined to a basic protein fraction, Cb (pI > 9.5) separable by DEAE-cellulose chromatography. Two proteins with molecular sizes close to 16,000 daltons were isolated from this fraction by preparative acidic gel electrophoresis in the presence of Triton X-100. One of the proteins (CbII) is lethal to mice (ld50 = 1 mg/kg) and shows phospholipase A activity as well as direct hemolytic activity. The other protein (CbI) does not reveal any known biological activity. However, upon recombination of the two a synergistic lethal activity is evident (the ld50 of the mixture = 0.25 mg/kg). It is suggested that CbI may be a specifier which potentiates the toxicity of the phospholipase A at the target site.
AB - R. Batzri-Izraeli and A. Bdolah. Isolation and characterization of the main toxic fraction from the venom of the false horned viper (Pseudocerastes fieldi). Toxicon 20, 867-875, 1982-The venom of Pseudocerastes fieldi was subjected to gel filtration on Sephadex G-75. Most of the protein and lethality of the venom were eluted in a major symmetrical peak (C). The lethality of this peak is confined to a basic protein fraction, Cb (pI > 9.5) separable by DEAE-cellulose chromatography. Two proteins with molecular sizes close to 16,000 daltons were isolated from this fraction by preparative acidic gel electrophoresis in the presence of Triton X-100. One of the proteins (CbII) is lethal to mice (ld50 = 1 mg/kg) and shows phospholipase A activity as well as direct hemolytic activity. The other protein (CbI) does not reveal any known biological activity. However, upon recombination of the two a synergistic lethal activity is evident (the ld50 of the mixture = 0.25 mg/kg). It is suggested that CbI may be a specifier which potentiates the toxicity of the phospholipase A at the target site.
UR - https://www.scopus.com/pages/publications/0020462796
U2 - 10.1016/0041-0101(82)90074-5
DO - 10.1016/0041-0101(82)90074-5
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AN - SCOPUS:0020462796
SN - 0041-0101
VL - 20
SP - 867
EP - 875
JO - Toxicon
JF - Toxicon
IS - 5
ER -