Quaternary structure of enzymes in trematodes of the genus Lecithochirium: inference from allozymic patterns

The quaternary structure of ten enzymes in hemiurid flukes of the genus Lecithochirium (Digenea, Hemiuridae) was inferred using allozyme electrophoresis. Allozyme variants with single-banded homozygotes and double-banded heterozygotes characteristic of monomeric enzymes were observed for aconitase, adenosine deaminase and phosphoglucomutase. The phenotypic variation (single-banded and triple-banded profiles) detected for glucose phosphate isomerase, isocitrate dehydrogenase, phosphogluconate dehydrogenase and malate dehydrogenase, suggest a dimeric structure for these enzymes. These results are consistent with structures already known for invertebrates, including parasitic helminths. Atypical heterozygote patterns were observed for fumarase and malic enzyme, both of which revealed monomeric profiles. Moreover, in the genus Lecithochirium, both monomeric and dimeric isozymes for hexokinase may be present. However, there are other possible explanations for the unusual triple-banded pattern detected for this enzyme. The results are discussed in the context of possible variations in subunit number of homologous enzymes within phylogenetically diverse groups such as parasitic helminths, and compared with those of previous studies using allozyme analysis.