Polyacrylamide gel electrophoresis reveals similar differences between the retinal-specific lactate dehydrogenase (LDH) isozymes of the salmon (Salmo salar L.) and the sea-trout (Salmo trutta forma trutta L.) as those previously described for the salmon and the brown trout (Salmo trutta L.). F~ salmon x sea-trout hybrids give a classic hybrid isozyme pattern, but the Fz hybrids all possess the parental sea-trout type pattern. Loss of part of the salmon genome in these latter hybrids is the most likely explanation. It was observed that when the individual eye isozymes of the salmon, the sea-trout, and the rainbow trout (Salmo gairdneri Richardson) were eluted from preparative polyacrylamide gels and re-electrophoresed, an apparent interconversion of certain isozyme bands occurred. This phenomenon was also evident using starch gel. However, the major cathodally migrating isozyme in each case (presumably the E4 isozyme) re-electrophoresed pure. The reasons for these interconversions are, as yet, unclear. Attempts to produce in vitro hybridization between the various isolated individual isozymes were unsuccessful Km pyruvate values for the different salmon isozymes were of the order expected from results already published for other teleosts.
INTRODUCTION 4
A number of investigators have shown that lactate dehydrogenase (E.C.