Abstract
Oxyhaemoglobins of six digenetic trematodes,--Srivastavaia indica, Gastrothylax crumenifer, Gigantocotyle explanatum, Fasciolopsis buski, Gastrodiscoides hominis, Isoparorchis hypselobagri, and of their 3 vertebrate hosts, Bubalus bubalis, Sus scrofa, Wallago attu, were subjected to alkali denaturation at a pH of 12.4. All oxyhaemoglobins from trematodes and their hosts differ from each other in the rate and extent of alkali denaturation which may be explained due to variations in the amino acid sequences of a particular haem protein in addition to other factors.
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