Preparation of a coral snake antivenin from goat serum

Kocholaty, Walter F.; Bowles-Ledford, Edith; Daly, Joyce G.; Billings, Thomas A.

doi:10.1016/0041-0101(71)90086-9

Cited by 9 publications

(2 citation statements)

References 4 publications

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“…Snake antivenom production takes several stages and therefore considerable amounts of venom, in order to guarantee the quality of the medicament [7–10]. First, the toxicity of the venoms used for immunization must be determined (e.g.…”

Section: Introductionmentioning

confidence: 99%

A polyvalent coral snake antivenom with broad neutralization capacity

et al. 2019

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Coral snakes of the genus Micrurus have a high diversity and wide distribution in the Americas. Despite envenomings by these animals being uncommon, accidents are often severe and may result in death. Producing an antivenom to treat these envenomings has been challenging since coral snakes are difficult to catch, produce small amounts of venom, and the antivenoms produced have shown limited cross neutralization. Here we present data of cross neutralization among monovalent antivenoms raised against M. dumerilii, M. isozonus, M. mipartitus and M. surinamensis and the development of a new polyvalent coral snake antivenom, resulting from the mix of monovalent antivenoms. Our results, show that this coral snake antivenom has high neutralizing potency and wide taxonomic coverage, constituting a possible alternative for a long sought Pan-American coral snake antivenom.

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Section: Introductionmentioning

confidence: 99%

A polyvalent coral snake antivenom with broad neutralization capacity

et al. 2019

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“…[8] noted that phospholipase A (EC 3.1.1.4) is widely distributed in the Colubridae, Elapidae, Viperidae and Crotalidae. Previously phospholipase A has been purified from several snake venoms [9-221 and the complete amino acid sequence was elucidated for the phospholipaseA isolated from the venoms of Bitis gabonica [23] and Naja melanoleuca [24].…”

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confidence: 99%

Hemachatus haemachatus (Ringhals) Venom. Purification, Some Properties and Amino‐Acid Sequence of Phospholipase A (Fraction DE‐I)

Joubert¹

1975

European Journal of Biochemistry

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Two isoenzymes of phospholipase A (fraction DE-I and DE-11) were isolated from the venom of Hemachatus haemachatus (Ringhals) by gel filtration on Sephadex G-50 and by ion-exchange chromatography on DEAE-cellulose. Fraction DE-I was homogeneous by various physicochemical criteria. The enzyme comprises 119 amino acid residues and is cross-linked by seven disulphide bridges. The values of the molecular weight of fraction DE-I from gel filtration in the presence of calcium ions, also by the dodecylsulphate gel method and calculated from the amino acid composition were close to 13 500. The complete amino acid sequence of phospholipase A (fraction DE-I) was elucidated. The reduced and S-carboxymethylated enzyme was digested with trypsin, chymotrypsin, thermolysin and subtilisin and the peptides purified by DEAE-cellulose chromatography, gel filtration and chromatography or electrophoresis on paper. The amino acid sequences of the intact enzyme and the pure peptides were determined by the Edman procedure, either through the use of the automatic sequencer or by manual manipulation. The chymotryptic digest provided the necessary overlapping peptides for aligning the tryptic peptides. The amino acid sequence of Hemachatus haemachatus phospholipase A (fraction DE-I) shows a high degree of homology with the three isoenzymes of phospholipase A from Naja melanoleuca and is also homologous with the phospholipase A from Bitis gabonica and porcine pancreas. and Porath [ 5 ] , with gel filtration, succeeded in obtaining four protein peaks from Ringhals venom. Phosphodiesterase, acetylcholine esterase, and 5'-nucleotidase appeared together in the first peak while lecithinase A was eluted in the second peak.In

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Therapeutic Antibodies to Snake Venoms

Theakston¹,

Smith²

1995

Therapeutic Antibodies

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Preparation of a coral snake antivenin from goat serum

Cited by 9 publications

References 4 publications

A polyvalent coral snake antivenom with broad neutralization capacity

A polyvalent coral snake antivenom with broad neutralization capacity

Hemachatus haemachatus (Ringhals) Venom. Purification, Some Properties and Amino‐Acid Sequence of Phospholipase A (Fraction DE‐I)

Therapeutic Antibodies to Snake Venoms

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