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An immunochemical analysis of the novel liver‐restricted LDH activity from cichlid fishes (Cichlidae: Teleostei) confirms its non‐orthology with piscine LDH‐C
Author(s) -
Leibel W. S.,
Bass K. N.,
Eshbach J. E.
Publication year - 1991
Publication title -
journal of fish biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.672
H-Index - 115
eISSN - 1095-8649
pISSN - 0022-1112
DOI - 10.1111/j.1095-8649.1991.tb05078.x
Subject(s) - cichlid , isozyme , biology , lactate dehydrogenase , teleostei , zoology , biochemistry , enzyme , fish <actinopterygii> , fishery
In an electrophoretic survey of lactate dehydrogenase (LDH) isozymes in neotropical cichlid fishes (Perciformes: Cichlidae) several species were discovered in which a cathodal liver‐restricted isozyme is expressed along with the highly anodal eye‐restricted isozyme (LDH‐C 4 ) typically encountered in perciform fishes. Biochemical characterization of these two isozymes from the basketmouth cichlid, Acaronia nassa (Heckel), strongly suggested that they were non‐orthologous and challenged the accepted view that eye‐ and liver‐restricted LDH isozymes are alternative expressions of the same (LDH‐C *) gene. In this study, antiserum raised against cypriniform (goldfish) liver‐restricted LDH‐C 4 failed to cross‐react with the basketmouth liver‐restricted analogue while effectively titrating the eye‐restricted, anodal isozyme and, at higher titres, the LDH‐B 4 , heart‐restricted isozyme from all cichlid species. Anti‐serum raised against basketmouth muscle‐restricted LDH‐A 4 failed to titrate any of the eye‐ and liver‐restricted isozymes. These data confirm the orthology of eye‐ and liver‐restricted LDH isozymes in Cypriniform and Perciform fishes as originally proposed, suggest that the liver‐restricted isozyme of cichlid fishes is non‐orthologous and further raise the question of identity and evolutionary origin of this anomalous LDH activity.