Lactate dehydrogenase isozyme patterns of fish
Journal of Experimental Zoology · 1965 · 483 citations · 25 references
Animal PhysiologyBiologyProtein SubunitsB SubunitsAquatic Food SystemBiochemistryMolecular EcologyNatural SciencesGeneticsEvolutionary BiologyLdh IsozymesMolecular GeneticsAquatic OrganismMetabolismMedicineAlcohol DehydrogenasesPhylogenetic Analysis
Abstract Representatives of 30 species of fish were examined for their content of LDH isozymes. One major isozyme system was found in all fish. In addition, two minor systems restricted to eyes and to gonads were found in many fish. Fish may be classified into four groups on the basis of their possession of one, two, three, or five major isozymes of LDH. The major isozyme patterns can be attributed to the polymers of two protein subunits under the control of two genes, as in mammals and birds, but the variety of heteropolymers produced varies in different species. The fluke and other flatfish are exceptional in that they synthesize only one kind of subunit which polymerizes to form a single variety of LDH. All other fish produced at least two major isozymes presumably the homopolymers of A and B subunits. The three‐isozyme fish produce, in addition, a single heteropolymer. A few fish produce three heteropolymers and two homopolymers to produce the characteristic pattern of five isozymes seen in mammals. In populations of the whiting, which has five major isozymes, two mutant alleles at the B locus were discovered. Each of these alleles produced polypeptides with characteristic electrophoretic mobilities. Consequently, heterozygous individuals contained more than 15 isozymes. A variety of minor isozymes that appear on zymograms may represent modifications of the major isozymes. However, the minor isozyme systems of the gonad and the eye seem to be genetically distinct molecular systems, separate from and in addition to the major isozyme system.
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