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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1988-4-11
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pubmed:databankReference | |
pubmed:abstractText |
The cDNA clones for rat aldolase C mRNA having the nearly complete length were isolated from a rat brain cDNA library and sequenced. The nucleotide sequence of pRAC2-1, a cDNA clone having the largest cDNA insert, indicates that the cDNA is composed of a 105-base-pair 5'-noncoding sequence, a 1089-base-pair coding-sequence and a 382-base-pair 3'-noncoding sequence. The amino acid sequence of aldolase C deduced from a possible open reading frame was composed of 362 residues having a relative molecular mass of 39,164 excluding the initiating methionine, one amino acid shorter than aldolases A and B. The length of aldolase c mRNA was 1750 residues, somewhat longer than that of the aldolase A and B transcripts. The aldolase C mRNA was distributed mainly in the brain, some in ascites hepatoma and fetal liver. Comparison of the amino acid sequences of rat aldolase C with those for rat aldolase A and B [Joh et al. (1985) Gene 39, 17-24; Tsutsumi et al. (1984) J. Biol. Chem. 259, 14572-14575], which have been determined previously, shows the existence of highly conserved stretches of amino acid among the three isozymic forms throughout their sequences. The extent of the homology between aldolases A and C is 81%, while those between aldolases A and B, and B and C are 70%, respectively. The analysis of amino acid substitution among aldolases A, B and C from several species suggests that the isozyme genes diverged much earlier than animal species appeared and that the aldolase C gene has evolved from the aldolase A gene after aldolase A and B genes diverged.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Transposable Elements,
http://linkedlifedata.com/resource/pubmed/chemical/Fructose-Bisphosphate Aldolase,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
171
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
471-8
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:2831050-Amino Acid Sequence,
pubmed-meshheading:2831050-Animals,
pubmed-meshheading:2831050-Base Sequence,
pubmed-meshheading:2831050-Biological Evolution,
pubmed-meshheading:2831050-Brain,
pubmed-meshheading:2831050-Chickens,
pubmed-meshheading:2831050-Cloning, Molecular,
pubmed-meshheading:2831050-DNA,
pubmed-meshheading:2831050-DNA Transposable Elements,
pubmed-meshheading:2831050-Drosophila,
pubmed-meshheading:2831050-Fructose-Bisphosphate Aldolase,
pubmed-meshheading:2831050-Genes,
pubmed-meshheading:2831050-Humans,
pubmed-meshheading:2831050-Isoenzymes,
pubmed-meshheading:2831050-Molecular Sequence Data,
pubmed-meshheading:2831050-RNA, Messenger,
pubmed-meshheading:2831050-Rabbits,
pubmed-meshheading:2831050-Rats,
pubmed-meshheading:2831050-Species Specificity
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pubmed:year |
1988
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pubmed:articleTitle |
The structure of brain-specific rat aldolase C mRNA and the evolution of aldolase isozyme genes.
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pubmed:affiliation |
Department of Biochemistry, Saga Medical School, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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