Analogy and homology of the dehydrogenases of Oomycetes. II. Regulation by GTP of D(−)lactic dehydrogenases and isozyme patterns

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Abstract
The presence and electrophoretic mobilities of D(−)lactic dehydrogenase isozymes was studied in 49 species of Oomycetes. The lactic dehydrogenase (LDH) isozymes were electro-phoretically similar in species of the following genera: Saprolegnia, Achlya, Protoachlya, and Isoachlya. There were moderate differences in electrophoretic mobilities of the isozymes of species of Aphanomyces, Aphanopsis, Thraustotheca, and Leptolegnia. Two species of Lepto-mitales were studied and the isozyme from Sapromyces elongatus was unique and distinct compared to all the other Oomycete D(−)LDH isozymes. It is present in large quantities (about 5% of cell protein) and is a highly cathodic protein. The isozymes of the genus Pythium displayed greater variation in electrophoretic mobilities, and in three cases, more than one isozyme species was present in the same organism. Leptolegnia caudata was the only other organism outside the Pythium spp. that had two isozymes.The isozymes of the genus Pythium were the most sensitive to allosteric inhibition by GTP.

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