EVOLUTION OF LACTATE-DEHYDROGENASE GENES
EVOLUTION OF LACTATE-DEHYDROGENASE GENES
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DOI:
10.1016/0014-5793(72)80675-6
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发表时间:
1972-01-01
期刊:
影响因子:
3.5
通讯作者:
HOLMES, RS
中科院分区:
文献类型:
--
作者:
HOLMES, RS
The enzyme lactate dehydrogenase (LDH) exists as a complex system in vertebrate organisms and is encoded in two major structural genes (A and B), each resulting in a different subunit of LDH [l-3]. These polypeptides usually assemble randomly to form five tetrameric isozymes (A4, A3 B, A* B2, AB3, and B4), although in certain fish, restriction in subunit assembly does occur and the expected five isozymes are not formed [4-71. A third locus (C) is present in mammals and birds and functions only in primary spermatocytes producing a distinct LDH-C4 isozyme [g-lo]. An additional structural gene (E) has been established in teleosts (bony fish) and is expressed in retinal and nervous tissue resulting in the synthesis of LDH-E4 as well as other isozymes containing A, B, and E polypeptide subunits [7, 111. Studies on LDH from gadoid fish (eg. haddock, cod) have shown the presence of an LDH isozyme specific to liver tissue. Genetic and evolutionary variation of the LDH isozymes in these fish indicate that this isozyme is encoded at a separate locus (F)[121. LDH from salmonid fish is determined by five gene loci [13, 141 resulting in the synthesis of more than fifteen isozymes in homozygous individuals. Cytological and biochemical studies have verified the existence of duplicated A (A and A’) and B (B and B’) loci in addition to the E locus in these fish [13-181. Immunochemical procedures have been found to be very useful in studies related to biochemical evolution and phylogeny [19-2 11. Antibodies to specific enzymes or isozymes may be used in the investigation of the structural similarities of gene products at different stages of evolution [20-221 or in establishing sub-