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http://purl.uniprot.org/citations/3418107http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/3418107http://www.w3.org/2000/01/rdf-schema#comment"Primary hyperoxaluria type 1 (PH1) is an inherited disorder of glyoxylate metabolism caused by a deficiency of the hepatic peroxisomal enzyme alanine: glyoxylate aminotransferase (AGT; EC 2.6.1.44) [FEBS Lett (1986) 201:20]. The aim of the present study was to investigate the intracellular distribution of immunoreactive AGT protein, using protein A-gold immunocytochemistry, in normal human liver and in livers of PH1 patients with (CRM+) or without (CRM-) immunologically crossreacting enzyme protein. In all CRM+ individuals, which included three controls, a PH1 heterozygote and a PH1 homozygote immunoreactive AGT protein was confined to peroxisomes, where it was randomly dispersed throughout the peroxisomal matrix with no obvious association with the peroxisomal membrane. No AGT protein could be detected in the peroxisomes or other cytoplasmic compartments in the livers of CRM-PH1 patients (homozygotes). The peroxisomal labeling density in the CRM+ PH1 patient, who was completely deficient in AGT enzyme activity, was similar to that of the controls. In addition, in the PH1 heterozygote, who had one third normal AGT enzyme activity, peroxisomal labeling density was reduced to 50% of normal."xsd:string
http://purl.uniprot.org/citations/3418107http://purl.org/dc/terms/identifier"doi:10.1177/36.10.3418107"xsd:string
http://purl.uniprot.org/citations/3418107http://purl.uniprot.org/core/author"Wise P.J."xsd:string
http://purl.uniprot.org/citations/3418107http://purl.uniprot.org/core/author"Danpure C.J."xsd:string
http://purl.uniprot.org/citations/3418107http://purl.uniprot.org/core/author"Guttridge K.M."xsd:string
http://purl.uniprot.org/citations/3418107http://purl.uniprot.org/core/author"Cooper P.J."xsd:string
http://purl.uniprot.org/citations/3418107http://purl.uniprot.org/core/date"1988"xsd:gYear
http://purl.uniprot.org/citations/3418107http://purl.uniprot.org/core/name"J Histochem Cytochem"xsd:string
http://purl.uniprot.org/citations/3418107http://purl.uniprot.org/core/pages"1285-1294"xsd:string
http://purl.uniprot.org/citations/3418107http://purl.uniprot.org/core/title"Immunocytochemical localization of human hepatic alanine: glyoxylate aminotransferase in control subjects and patients with primary hyperoxaluria type 1."xsd:string
http://purl.uniprot.org/citations/3418107http://purl.uniprot.org/core/volume"36"xsd:string
http://purl.uniprot.org/citations/3418107http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/3418107
http://purl.uniprot.org/citations/3418107http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/3418107
http://purl.uniprot.org/uniprot/P21549#attribution-7A1517198A3A75CA6405816870AA2F16http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/3418107