Electrophoretic Analysis of Enzymes from Three Species of Chlamydomonas

Abstract

A B S T RAe T Isoenzyme patterns of acetone-extracted proteins revealed a close similarity between Chlamydomonas eugametos and C. moewusii but a distant relationship between the two and C. reinhardtii. Chlamydomonas eugametos and C. moewusii had identical banding patterns of malate dehydrogenase (MDH) and leucine aminopeptidase (LAP) in starch gels. These two species exhibited the same MDH distribution spectrum in analytical disc polyacrylamide gels but neither species showed definitive LAP or glutamate dehydrogenase (GDH) activity. There were differences in the starch gel alpha esterase (a-EST) patterns of C. eugametos and C. moewu.sii due to an additional weak band at Rf 0.75 in the latter species and a slight variation in the position of another band at Rf 0.80-0.82. Some variations between the two species also occurred in the a-EST banding in disc gels at Rf 0.70-0.85 and at Rf 0.06-0.14 with C. moewusii exhibiting the greatest number of bands. Chlamydomonas reinhardtii displayed patterns of all four enzymes but the band characteristics were distinctively different from those of C. euqameios and C. moewusii. There appeared to be no obvious isoenzyme difference between mating types of either species. It is concluded that C. eugametos and C. moewusii are not identical species but are closely related in regard to the enzymes assayed. Isoenzyme analysis is considered to be a useful approach to algal systematics.