Coexpression of distinct eye- and liver-specific LDH isozymes in cichlid fish

In a recent electrophoretic survey of lactate dehydrogenase (LDH) in neotropical cichlid fishes (Perciformes, Cichlidae) we have discovered several species in which a cathodal liver-specific isozyme is expressed along with the highly-anodal eye-specific isozyme (LDH-C4) typically encountered in perciform fishes. We believe this fourth, liver-specific LDH isozyme to be real and not artifactual since homogenization of fresh liver from one of these species, the Basketmouth cichlid (Acaronia nassa), in either of two nondenaturing detergents or in the presence of the protease inhibitor phenylmethylsulfonylfluoride affects neither the presence nor mobility of this cathodal band. Moreover, it continues to be expressed in the captively bred F1 of these same wild fish. The discovery of several fish species, like the Basketmouth, in which biochemically distinct eye- and liver-specific LDH isozymes are coexpressed, is discussed in light of the currently accepted hypothesis that these two isozymes are encoded by a single locus (LDH-C) which has undergone divergent tissue expression in several other major teleost groups. Preliminary characterization of the liver-specific isozyme relative to the eye-specific LDH-C4 in the Basketmouth cichlid with respect to thermolability and NADH-induced binding to oxamate-sepharose columns suggests that the eye- and liver-specific LDH isozymes are biochemically quite distinct in this fish and that they are probably encoded by two distinct loci.