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http://purl.uniprot.org/citations/9148925http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9148925http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9148925http://www.w3.org/2000/01/rdf-schema#comment"CD45 is an abundant, highly glycosylated transmembrane protein-tyrosine phosphatase expressed on hematopoietic cells. Herein we demonstrate that two proteins of 116 kDa and 80 kDa copurify with CD45 from mouse T cells. Microsequence analysis of the 116-kDa protein revealed high similarity to an incomplete human open reading frame that has been suggested to correspond to the catalytic alpha-subunit of glucosidase II. We determined the nucleotide sequence of the mouse cDNA and observed that it encodes a protein product nearly identical to its human homologue and shares an active site consensus sequence with Family 31 glucosidases. Amino acid sequencing of the 80-kDa protein, followed by molecular cloning, revealed high homology to human and bovine cDNAs postulated to encode the beta-subunit of glucosidase II. Antisera developed to the mouse beta-subunit allowed us to demonstrate that the interaction between CD45 and glucosidase II can be reconstituted in vitro in an endoglycosidase H-sensitive manner. The strong interaction between glucosidase II and CD45 may provide a paradigm for investigating novel aspects of the biology of these proteins."xsd:string
http://purl.uniprot.org/citations/9148925http://purl.org/dc/terms/identifier"doi:10.1074/jbc.272.20.13117"xsd:string
http://purl.uniprot.org/citations/9148925http://purl.org/dc/terms/identifier"doi:10.1074/jbc.272.20.13117"xsd:string
http://purl.uniprot.org/citations/9148925http://purl.uniprot.org/core/author"Ostergaard H.L."xsd:string
http://purl.uniprot.org/citations/9148925http://purl.uniprot.org/core/author"Ostergaard H.L."xsd:string
http://purl.uniprot.org/citations/9148925http://purl.uniprot.org/core/author"Arendt C.W."xsd:string
http://purl.uniprot.org/citations/9148925http://purl.uniprot.org/core/author"Arendt C.W."xsd:string
http://purl.uniprot.org/citations/9148925http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9148925http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9148925http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/9148925http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/9148925http://purl.uniprot.org/core/pages"13117-13125"xsd:string
http://purl.uniprot.org/citations/9148925http://purl.uniprot.org/core/pages"13117-13125"xsd:string
http://purl.uniprot.org/citations/9148925http://purl.uniprot.org/core/title"Identification of the CD45-associated 116-kDa and 80-kDa proteins as the alpha- and beta-subunits of alpha-glucosidase II."xsd:string
http://purl.uniprot.org/citations/9148925http://purl.uniprot.org/core/title"Identification of the CD45-associated 116-kDa and 80-kDa proteins as the alpha- and beta-subunits of alpha-glucosidase II."xsd:string
http://purl.uniprot.org/citations/9148925http://purl.uniprot.org/core/volume"272"xsd:string
http://purl.uniprot.org/citations/9148925http://purl.uniprot.org/core/volume"272"xsd:string
http://purl.uniprot.org/citations/9148925http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9148925
http://purl.uniprot.org/citations/9148925http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9148925
http://purl.uniprot.org/citations/9148925http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9148925
http://purl.uniprot.org/citations/9148925http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9148925
http://purl.uniprot.org/uniprot/P06800http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/9148925
http://purl.uniprot.org/uniprot/Q8BHN3http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/9148925