Comparison of the Esterases and Acid Phosphatases in Paramecium multimicronucleatum , Syngens 1–5, P. jenningsi, P. caudatum , and the P. aurelia Complex 1

Abstract

Forty-eight stocks in Paramecium jenningsi , syngens 1–5 of P. multimicronucleatum, P. caudatum, P. primaurelia, P. biaurelia , and P. tetraurelia were grown axenically and tested for their esterases and acid phosphatases using starch gel electrophoresis. The five esterases and the acid phosphatases previously characterized in species of the P. aurelia complex were also found in P. jenningsi , and three to four of the esterases and the acid phosphatases were found in the P. multimicronucleatum species complex and in P. caudatum . Additional subtypes were observed for each of the enzyme phenotypes in these new (though here unnamed) species of Paramecium . Two of the new acid phosphatase subtypes, which depart radically in mobility and in pattern, were found in syngen 3 of P. multimicronucleatum and in P. caudatum . Except for syngens 1 and 5 in P. multimicronucleatum , the degree of similarity between syngens 1, 5 and 2, 3, and 4 appears to be very low—perhaps even lower than that seen for species in the aurelia complex. More realistically, the syngens of P. multimicronucleatum should be considered as separate species although they are not here given separate taxonomic names. Limited sharing of subtypes occurred between species in different species complexes. This observation suggests that the molecular distances between species complexes may be even greater than between species within a complex.