Erabutoxin a was partially hydrolysed with enzymes and sulphuric acid and the resulting peptides were separated from each other by column chromatography and paper electrophoresis. From the results of amino acid analyses of the sulphur-containing peptides and their oxidized components, all four disulphide bridges in the toxin molecule were located. The disulphide bonds were found between half-cystine residues at positions 3 and 24, 17 and 41, 43 and 54, and 55 and 60 from the N-terminus.
| Predicate | Object |
|---|---|
| rdf:type | |
| rdfs:comment |
Erabutoxin a was partially hydrolysed with enzymes and sulphuric acid and the resulting peptides were separated from each other by column chromatography and paper electrophoresis. From the results of amino acid analyses of the sulphur-containing peptides and their oxidized components, all four disulphide bridges in the toxin molecule were located. The disulphide bonds were found between half-cystine residues at positions 3 and 24, 17 and 41, 43 and 54, and 55 and 60 from the N-terminus.
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| skos:exactMatch | |
| uniprot:name |
Biochem. J.
|
| uniprot:author |
Endo Y.,
Ishii S.,
Sato S.,
Tamiya N.
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| uniprot:date |
1971
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| uniprot:pages |
463-467
|
| uniprot:title |
The disulphide bonds of erabutoxin a, a neurotoxic protein of a sea-snake (Laticauda semifasciata) venom.
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| uniprot:volume |
122
|