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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1992-2-27
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pubmed:databankReference |
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pubmed:abstractText |
cDNA clone for human liver S-adenosylmethionine synthetase (liver-specific isoenzyme) was isolated from a cDNA library of human liver poly(A)+ RNA. The cDNA sequence encoded a polypeptide consisting of 395 amino acid residues with a calculated molecular mass of 43675 Da. Alignment of the predicted amino acid sequence of this protein with that of rat liver S-adenosylmethionine synthetase showed a high degree of similarity. The coding region of the human liver S-adenosylmethionine synthetase cDNA sequence was 89% identical at the nucleotide level and 95% identical at the amino acid level to the sequence for rat liver S-adenosylmethionine synthetase.
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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 |
Sep
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pubmed:issn |
0158-5231
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
25
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
81-90
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:1772450-Amino Acid Sequence,
pubmed-meshheading:1772450-Animals,
pubmed-meshheading:1772450-Base Sequence,
pubmed-meshheading:1772450-Cloning, Molecular,
pubmed-meshheading:1772450-DNA,
pubmed-meshheading:1772450-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1772450-Humans,
pubmed-meshheading:1772450-Immunoblotting,
pubmed-meshheading:1772450-Kidney,
pubmed-meshheading:1772450-Liver,
pubmed-meshheading:1772450-Methionine Adenosyltransferase,
pubmed-meshheading:1772450-Molecular Sequence Data,
pubmed-meshheading:1772450-Molecular Weight,
pubmed-meshheading:1772450-Rats,
pubmed-meshheading:1772450-Restriction Mapping,
pubmed-meshheading:1772450-Sequence Alignment
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pubmed:year |
1991
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pubmed:articleTitle |
Molecular cloning and nucleotide sequence of cDNA encoding the human liver S-adenosylmethionine synthetase.
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pubmed:affiliation |
Department of Pathological Biochemistry, Tokyo Medical and Dental University, Japan.
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pubmed:publicationType |
Journal Article
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