Differing stabilities of snake venom cardiotoxins in acidic aqueous acetonitrile.
1. Although snake venom cardiotoxins constitute a homologous family of proteins, subclasses with different structural and biological properties exist. 2. By using circular dichroism spectroscopy of twelve cardiotoxins belonging to two structural classes and one non-classified group, this investigation indicated that cardiotoxins differ in their stabilities towards denaturation in acidic aqueous acetonitrile, as used in some reversed-phase high performance liquid chromatography separations. 3. It was also shown that cardiotoxins of the structural class II are in general less stable towards this denaturation than class I and non-classified cardiotoxins.
Osthoff
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Division of Processing and Chemical Manufacturing Technology, CSIR, Pretoria, Republic of South Africa.
D000097:Acetonitriles; D000818:Animals; D002942:Circular Dichroism; D004179:Cobra Cardiotoxin Proteins / Q000145:classification; D004546:Elapid Venoms / Q000145:classification; D011489:Protein Denaturation; D012997:Solvents; D014269:Trifluoroacetic Acid
D000097:Acetonitriles; D004179:Cobra Cardiotoxin Proteins; D004546:Elapid Venoms; D012997:Solvents; D014269:Trifluoroacetic Acid