Abstract:
:A cDNA that encodes the heart-type lactate dehydrogenase (LDH-B) from the teleost fish Fundulus heteroclitus was cloned and sequenced. The protein encoded by the cDNA was analyzed in relation to 13 LDH proteins from a variety of taxa. One of the deductions from this analysis is that LDH-B proteins have residues in the active site that are unique and that may be important in determining the biochemistry of the heart-type isozyme. Phylogenetic analysis of the LDH sequences indicates that the branch lengths are greater in lower vertebrates, suggesting that the amino acid replacement rates vary depending on the evolutionary constraints within each taxon. Furthermore, the analysis suggests that LDH-C arose prior to the divergence of the LDH-A and LDH-B isozymes and thus that it is probably ancestral to these isozymes.
journal_name
Mol Biol Evoljournal_title
Molecular biology and evolutionauthors
Crawford DL,Constantino HR,Powers DAdoi
10.1093/oxfordjournals.molbev.a040559subject
Has Abstractpub_date
1989-07-01 00:00:00pages
369-83issue
4eissn
0737-4038issn
1537-1719journal_volume
6pub_type
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