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Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
1994-4-26
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pubmed:abstractText |
Systematic molecular analysis of a Japanese class 1 glucose-6-phosphate dehydrogenase (G6PD) variant (G6PD Kobe) cDNA revealed a unique nucleotide substitution (1318 C to T) in exon 11, which predicts a substitution of leucine for phenylalanine at residue 440. This substitution is located in a region surrounding the putative structural NADP-binding domain. The markedly abnormal kinetics of glucose-6-phosphate (G6P) of G6PD Kobe suggest the interaction between both NADP and G6P binding sites.
|
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Feb
|
pubmed:issn |
0361-8609
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
45
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
|
pubmed:pagination |
185-6
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading | |
pubmed:year |
1994
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pubmed:articleTitle |
Molecular abnormality of a unique Japanese glucose-6-phosphate dehydrogenase variant (G6PD Kobe) with a greatly increased affinity for galactose-6-phosphate.
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pubmed:affiliation |
Okinaka Memorial Institute for Medical Research, Tokyo, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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