A combination of hybridization (in vivo and in vitro), immunochemical, and electrophoretic analyses reveals that both smallmouth bass, Micropterus dolomieui (Lacépède), and largemouth bass, M. salmoides (Lacépède), possess three homopolymeric lactate dehydrogenase (LDH) isozymes, A4, B4, and E4. The retinal-specific E4 isozymes of these two parental species possess different electrophoretic mobilities. The two bass species were hybridized to produce the interspecific F1 hybrids. In addition, F2 and F3 hybrid generations were produced. The genetic data from these crosses indicate that the retinal-specific LDH isozyme is the product of a distinct nuclear gene (E locus) on an autosomal chromosome. This E gene appears to segregate independently of the gene for supernatant MDH. The LDH E gene is highly active in the bass neural retina and less active in other neural tissues. However, unlike in most teleosts, the bass LDH E gene also functions in such nonneural tissues as the heart and kidney.
ASJC Scopus subject areas
- Ecology, Evolution, Behavior and Systematics
- Molecular Biology