Abstract

The conformation of allergen A from Ascaris suum has been studied by circular dichroism and i.r. spectroscopy. The native allergen has an alpha-helical content of over 50 per cent and may also contain some β-structure. This high proportion of ordered structure may account for its resistance to chemical and enzyme attack. After denaturation in alkali, the α-helices are largely absent, but some β-structure may remain.

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