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http://purl.uniprot.org/citations/1524427http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1524427http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1524427http://www.w3.org/2000/01/rdf-schema#comment"Two cDNAs which correspond to two very similar Class I aldolases have been isolated from a pea (Pisum sativum L.) cDNA library. With the exception of one codon they match the experimentally determined N-terminal sequence of a pea chloroplast aldolase. The deduced C-terminal sequence of one of these clones is unique among Class I aldolases. The deduced C-terminus of the other is more like the C-terminus of other eucaryotic Class I aldolases. Comparisons of sequence homology suggest that the pea chloroplast isozymes are only marginally more closely related to the anaerobically induced plant aldolases than to aldolases from animals."xsd:string
http://purl.uniprot.org/citations/1524427http://purl.org/dc/terms/identifier"doi:10.1016/0003-9861(92)90112-a"xsd:string
http://purl.uniprot.org/citations/1524427http://purl.org/dc/terms/identifier"doi:10.1016/0003-9861(92)90112-a"xsd:string
http://purl.uniprot.org/citations/1524427http://purl.uniprot.org/core/author"Heinrikson R.L."xsd:string
http://purl.uniprot.org/citations/1524427http://purl.uniprot.org/core/author"Heinrikson R.L."xsd:string
http://purl.uniprot.org/citations/1524427http://purl.uniprot.org/core/author"Morris P.W."xsd:string
http://purl.uniprot.org/citations/1524427http://purl.uniprot.org/core/author"Morris P.W."xsd:string
http://purl.uniprot.org/citations/1524427http://purl.uniprot.org/core/author"Anderson L.E."xsd:string
http://purl.uniprot.org/citations/1524427http://purl.uniprot.org/core/author"Anderson L.E."xsd:string
http://purl.uniprot.org/citations/1524427http://purl.uniprot.org/core/author"Razdan K."xsd:string
http://purl.uniprot.org/citations/1524427http://purl.uniprot.org/core/author"Razdan K."xsd:string
http://purl.uniprot.org/citations/1524427http://purl.uniprot.org/core/author"Zurcher-Neely H."xsd:string
http://purl.uniprot.org/citations/1524427http://purl.uniprot.org/core/author"Zurcher-Neely H."xsd:string
http://purl.uniprot.org/citations/1524427http://purl.uniprot.org/core/date"1992"xsd:gYear
http://purl.uniprot.org/citations/1524427http://purl.uniprot.org/core/date"1992"xsd:gYear
http://purl.uniprot.org/citations/1524427http://purl.uniprot.org/core/name"Arch. Biochem. Biophys."xsd:string
http://purl.uniprot.org/citations/1524427http://purl.uniprot.org/core/name"Arch. Biochem. Biophys."xsd:string
http://purl.uniprot.org/citations/1524427http://purl.uniprot.org/core/pages"192-197"xsd:string
http://purl.uniprot.org/citations/1524427http://purl.uniprot.org/core/pages"192-197"xsd:string
http://purl.uniprot.org/citations/1524427http://purl.uniprot.org/core/title"Chloroplast and cytoplasmic enzymes: isolation and sequencing of cDNAs coding for two distinct pea chloroplast aldolases."xsd:string
http://purl.uniprot.org/citations/1524427http://purl.uniprot.org/core/title"Chloroplast and cytoplasmic enzymes: isolation and sequencing of cDNAs coding for two distinct pea chloroplast aldolases."xsd:string
http://purl.uniprot.org/citations/1524427http://purl.uniprot.org/core/volume"298"xsd:string
http://purl.uniprot.org/citations/1524427http://purl.uniprot.org/core/volume"298"xsd:string