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http://purl.uniprot.org/citations/10211631http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10211631http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10211631http://www.w3.org/2000/01/rdf-schema#comment"

Objective

We report a case showing an atypical lactate dehydrogenase (LD) isoenzyme pattern involving deficiency only of LD-1 and LD-2 in serum and erythrocytes. LD activity in serum from this patient was extremely low, similar to complete LD-H deficiency, and also that in erythrocytes was low.

Design

The DNA fragment containing exon 1 through 7 of the LD-H gene were amplified by PCR and directly sequenced. Total RNA was prepared from venous blood and the proportion of LD-H cDNA to total LD cDNA was semiquantified.

Results

Genetic analysis by DNA sequencing detected a three base deletion (AAT) at codon 220 of exon 5, which caused a deletion of one asparagine. The present case did not show reduced LD-H expression at the mRNA level in whole blood. Residue 220 is involved in turning beta-J to alpha1-G and is not buried in the interior of the protein. The novel homozygous in-frame deletion mutation at codon 220 may cause a three-dimensional change of the subunit-binding domain."xsd:string
http://purl.uniprot.org/citations/10211631http://purl.org/dc/terms/identifier"doi:10.1016/s0009-9120(98)00097-6"xsd:string
http://purl.uniprot.org/citations/10211631http://purl.org/dc/terms/identifier"doi:10.1016/s0009-9120(98)00097-6"xsd:string
http://purl.uniprot.org/citations/10211631http://purl.uniprot.org/core/author"Kawano K."xsd:string
http://purl.uniprot.org/citations/10211631http://purl.uniprot.org/core/author"Kawano K."xsd:string
http://purl.uniprot.org/citations/10211631http://purl.uniprot.org/core/author"Maekawa M."xsd:string
http://purl.uniprot.org/citations/10211631http://purl.uniprot.org/core/author"Maekawa M."xsd:string
http://purl.uniprot.org/citations/10211631http://purl.uniprot.org/core/author"Sudo K."xsd:string
http://purl.uniprot.org/citations/10211631http://purl.uniprot.org/core/author"Sudo K."xsd:string
http://purl.uniprot.org/citations/10211631http://purl.uniprot.org/core/author"Okuda T."xsd:string
http://purl.uniprot.org/citations/10211631http://purl.uniprot.org/core/author"Okuda T."xsd:string
http://purl.uniprot.org/citations/10211631http://purl.uniprot.org/core/author"Akizuki S."xsd:string
http://purl.uniprot.org/citations/10211631http://purl.uniprot.org/core/author"Akizuki S."xsd:string
http://purl.uniprot.org/citations/10211631http://purl.uniprot.org/core/author"Magara T."xsd:string
http://purl.uniprot.org/citations/10211631http://purl.uniprot.org/core/author"Magara T."xsd:string
http://purl.uniprot.org/citations/10211631http://purl.uniprot.org/core/author"Houki N."xsd:string
http://purl.uniprot.org/citations/10211631http://purl.uniprot.org/core/author"Houki N."xsd:string
http://purl.uniprot.org/citations/10211631http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10211631http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10211631http://purl.uniprot.org/core/name"Clin. Biochem."xsd:string
http://purl.uniprot.org/citations/10211631http://purl.uniprot.org/core/name"Clin. Biochem."xsd:string
http://purl.uniprot.org/citations/10211631http://purl.uniprot.org/core/pages"137-141"xsd:string
http://purl.uniprot.org/citations/10211631http://purl.uniprot.org/core/pages"137-141"xsd:string
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