Hybrids between Schistosoma mansoni and S. rodhaini: characterization by isoelectric focusing of six enzymes.

Results are reported of enzyme analyses by isoelectric focusing in polyacrylamide gels of individual extracts from Schistosoma mansoni (Guadeloupe), S. rodhaini (Burundi), and their experimental hybrids (first and second generation). The distinctive patterns of lactate dehydrogenase (LDH), malate dehydrogenase (MDH), glucose-6-phosphate dehydrogenase (G6PD), acid phosphatase (AcP), phosphoglucomutase (PGM) and glucose phosphate isomerase (GPI) enable the characterization of the two parental strains and the hybrids. Particular observations, such as the existence of a polymorphism at both MDH-1 and MDH-2 loci and a sex-linked heredity for GPI, are discussed. A genetic interpretation is proposed to explain the patterns observed for MDH and GPI (with a dimeric structure) and for PGM (monomeric structure); a comparison is made with electrophoretic data available for S. mansoni and S. rodhaini.