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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1985-7-17
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pubmed:databankReference |
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pubmed:abstractText |
The complete covalent structure of the 331 amino acids of mouse lactate dehydrogenase (LDH) A4 isozyme has been determined by sequence analyses of both the protein and the genomic DNA. The mouse LDH-A gene spans a length of at least 7000 bases from the translation initiation codon ATG to the end of the 3' untranslated region, and it contains six introns that interrupt the protein-coding sequence. The relationships between the exon-intron organization of LDH-A gene and the structural-functional domains of the protein are discussed.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0014-2956
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
149
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
215-25
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:3996406-Amino Acid Sequence,
pubmed-meshheading:3996406-Animals,
pubmed-meshheading:3996406-Base Sequence,
pubmed-meshheading:3996406-Cloning, Molecular,
pubmed-meshheading:3996406-Genes,
pubmed-meshheading:3996406-Isoenzymes,
pubmed-meshheading:3996406-L-Lactate Dehydrogenase,
pubmed-meshheading:3996406-Mice,
pubmed-meshheading:3996406-Mice, Inbred DBA,
pubmed-meshheading:3996406-Peptide Fragments,
pubmed-meshheading:3996406-Protein Biosynthesis,
pubmed-meshheading:3996406-Protein Conformation,
pubmed-meshheading:3996406-Species Specificity,
pubmed-meshheading:3996406-Swine
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pubmed:year |
1985
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pubmed:articleTitle |
Protein structure and gene organization of mouse lactate dehydrogenase-A isozyme.
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pubmed:publicationType |
Journal Article
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