PubMed:8288556 JSONTXT

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":93},"obj":"Sentence"},{"id":"T2","span":{"begin":94,"end":257},"obj":"Sentence"},{"id":"T3","span":{"begin":258,"end":376},"obj":"Sentence"},{"id":"T4","span":{"begin":377,"end":564},"obj":"Sentence"},{"id":"T5","span":{"begin":565,"end":755},"obj":"Sentence"},{"id":"T6","span":{"begin":756,"end":954},"obj":"Sentence"},{"id":"T7","span":{"begin":955,"end":1140},"obj":"Sentence"},{"id":"T8","span":{"begin":1141,"end":1283},"obj":"Sentence"},{"id":"T9","span":{"begin":1284,"end":1474},"obj":"Sentence"},{"id":"T10","span":{"begin":1475,"end":1796},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":93},"obj":"Sentence"},{"id":"T2","span":{"begin":94,"end":257},"obj":"Sentence"},{"id":"T3","span":{"begin":258,"end":376},"obj":"Sentence"},{"id":"T4","span":{"begin":377,"end":564},"obj":"Sentence"},{"id":"T5","span":{"begin":565,"end":755},"obj":"Sentence"},{"id":"T6","span":{"begin":756,"end":954},"obj":"Sentence"},{"id":"T7","span":{"begin":955,"end":1140},"obj":"Sentence"},{"id":"T8","span":{"begin":1141,"end":1283},"obj":"Sentence"},{"id":"T9","span":{"begin":1284,"end":1474},"obj":"Sentence"},{"id":"T10","span":{"begin":1475,"end":1796},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Identification of probasin-related antigen as cystathionine gamma-lyase by molecular cloning.\nWe reported previously that a monoclonal antibody against probasin (rat prostatic secretory protein) recognizes a 40-kDa protein localized in rat liver and kidney. The protein (probasin-related antigen, PRB-RA) may participate in a specific differentiated function of these tissues. To clarify the molecular nature of PRB-RA, a series of cDNA clones coding for the protein were isolated from a rat liver expression library using an affinity-purified polyclonal antibody. The amino acid sequence deduced from the determined cDNA sequence included sequences identical with those of proteolytic fragments of PRB-RA, which covered about 70% of the deduced sequence. Northern blot hybridization of poly(A)+ RNA isolated from rat tissues showed the presence of predominant and minor mRNA species of about 2.0 and 4.3 kilobases, respectively, in the liver and kidney. A sequence homology search revealed that PRB-RA is almost completely identical to rat cystathionine gamma-lyase (cystathionase) and that it does not show overall homology with probasin. Three candidates for an epitope common to probasin and PRB-RA were found on close examination of the amino acid sequences of the two proteins. A synthetic peptide, TYFRRI, corresponding to one of the candidates, neutralized the reactivity of the anti-probasin monoclonal antibody to both probasin and PRB-RA on Western blot analysis. These results show that PRB-RA/cystathionase is neither structurally nor functionally related to probasin except for a common epitope and that cystathionase, a cystein-producing enzyme, is localized in urinary tubular epithelial cells in a highly restricted region of the kidney in addition to in liver parenchymal cells."}

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":166,"end":175},"obj":"http://purl.obolibrary.org/obo/MAT_0000078"},{"id":"T2","span":{"begin":240,"end":245},"obj":"http://purl.obolibrary.org/obo/MAT_0000097"},{"id":"T3","span":{"begin":250,"end":256},"obj":"http://purl.obolibrary.org/obo/MAT_0000119"},{"id":"T4","span":{"begin":492,"end":497},"obj":"http://purl.obolibrary.org/obo/MAT_0000097"},{"id":"T5","span":{"begin":937,"end":942},"obj":"http://purl.obolibrary.org/obo/MAT_0000097"},{"id":"T6","span":{"begin":947,"end":953},"obj":"http://purl.obolibrary.org/obo/MAT_0000119"},{"id":"T7","span":{"begin":1747,"end":1753},"obj":"http://purl.obolibrary.org/obo/MAT_0000119"},{"id":"T8","span":{"begin":1772,"end":1777},"obj":"http://purl.obolibrary.org/obo/MAT_0000097"}],"text":"Identification of probasin-related antigen as cystathionine gamma-lyase by molecular cloning.\nWe reported previously that a monoclonal antibody against probasin (rat prostatic secretory protein) recognizes a 40-kDa protein localized in rat liver and kidney. The protein (probasin-related antigen, PRB-RA) may participate in a specific differentiated function of these tissues. To clarify the molecular nature of PRB-RA, a series of cDNA clones coding for the protein were isolated from a rat liver expression library using an affinity-purified polyclonal antibody. The amino acid sequence deduced from the determined cDNA sequence included sequences identical with those of proteolytic fragments of PRB-RA, which covered about 70% of the deduced sequence. Northern blot hybridization of poly(A)+ RNA isolated from rat tissues showed the presence of predominant and minor mRNA species of about 2.0 and 4.3 kilobases, respectively, in the liver and kidney. A sequence homology search revealed that PRB-RA is almost completely identical to rat cystathionine gamma-lyase (cystathionase) and that it does not show overall homology with probasin. Three candidates for an epitope common to probasin and PRB-RA were found on close examination of the amino acid sequences of the two proteins. A synthetic peptide, TYFRRI, corresponding to one of the candidates, neutralized the reactivity of the anti-probasin monoclonal antibody to both probasin and PRB-RA on Western blot analysis. These results show that PRB-RA/cystathionase is neither structurally nor functionally related to probasin except for a common epitope and that cystathionase, a cystein-producing enzyme, is localized in urinary tubular epithelial cells in a highly restricted region of the kidney in addition to in liver parenchymal cells."}

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":166,"end":175},"obj":"Body_part"},{"id":"T2","span":{"begin":240,"end":245},"obj":"Body_part"},{"id":"T3","span":{"begin":250,"end":256},"obj":"Body_part"},{"id":"T4","span":{"begin":492,"end":497},"obj":"Body_part"},{"id":"T5","span":{"begin":937,"end":942},"obj":"Body_part"},{"id":"T6","span":{"begin":947,"end":953},"obj":"Body_part"},{"id":"T7","span":{"begin":1747,"end":1753},"obj":"Body_part"},{"id":"T8","span":{"begin":1772,"end":1777},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000078"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000097"},{"id":"A3","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000119"},{"id":"A4","pred":"mat_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MAT_0000097"},{"id":"A5","pred":"mat_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MAT_0000097"},{"id":"A6","pred":"mat_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/MAT_0000119"},{"id":"A7","pred":"mat_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/MAT_0000119"},{"id":"A8","pred":"mat_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/MAT_0000097"}],"text":"Identification of probasin-related antigen as cystathionine gamma-lyase by molecular cloning.\nWe reported previously that a monoclonal antibody against probasin (rat prostatic secretory protein) recognizes a 40-kDa protein localized in rat liver and kidney. The protein (probasin-related antigen, PRB-RA) may participate in a specific differentiated function of these tissues. To clarify the molecular nature of PRB-RA, a series of cDNA clones coding for the protein were isolated from a rat liver expression library using an affinity-purified polyclonal antibody. The amino acid sequence deduced from the determined cDNA sequence included sequences identical with those of proteolytic fragments of PRB-RA, which covered about 70% of the deduced sequence. Northern blot hybridization of poly(A)+ RNA isolated from rat tissues showed the presence of predominant and minor mRNA species of about 2.0 and 4.3 kilobases, respectively, in the liver and kidney. A sequence homology search revealed that PRB-RA is almost completely identical to rat cystathionine gamma-lyase (cystathionase) and that it does not show overall homology with probasin. Three candidates for an epitope common to probasin and PRB-RA were found on close examination of the amino acid sequences of the two proteins. A synthetic peptide, TYFRRI, corresponding to one of the candidates, neutralized the reactivity of the anti-probasin monoclonal antibody to both probasin and PRB-RA on Western blot analysis. These results show that PRB-RA/cystathionase is neither structurally nor functionally related to probasin except for a common epitope and that cystathionase, a cystein-producing enzyme, is localized in urinary tubular epithelial cells in a highly restricted region of the kidney in addition to in liver parenchymal cells."}

{"project":"HP-phenotype","denotations":[{"id":"T1","span":{"begin":301,"end":303},"obj":"Phenotype"},{"id":"T2","span":{"begin":416,"end":418},"obj":"Phenotype"},{"id":"T3","span":{"begin":703,"end":705},"obj":"Phenotype"},{"id":"T4","span":{"begin":1000,"end":1002},"obj":"Phenotype"},{"id":"T5","span":{"begin":1200,"end":1202},"obj":"Phenotype"},{"id":"T6","span":{"begin":1446,"end":1448},"obj":"Phenotype"},{"id":"T7","span":{"begin":1503,"end":1505},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0001370"},{"id":"A2","pred":"hp_id","subj":"T2","obj":"HP:0001370"},{"id":"A3","pred":"hp_id","subj":"T3","obj":"HP:0001370"},{"id":"A4","pred":"hp_id","subj":"T4","obj":"HP:0001370"},{"id":"A5","pred":"hp_id","subj":"T5","obj":"HP:0001370"},{"id":"A6","pred":"hp_id","subj":"T6","obj":"HP:0001370"},{"id":"A7","pred":"hp_id","subj":"T7","obj":"HP:0001370"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"Identification of probasin-related antigen as cystathionine gamma-lyase by molecular cloning.\nWe reported previously that a monoclonal antibody against probasin (rat prostatic secretory protein) recognizes a 40-kDa protein localized in rat liver and kidney. The protein (probasin-related antigen, PRB-RA) may participate in a specific differentiated function of these tissues. To clarify the molecular nature of PRB-RA, a series of cDNA clones coding for the protein were isolated from a rat liver expression library using an affinity-purified polyclonal antibody. The amino acid sequence deduced from the determined cDNA sequence included sequences identical with those of proteolytic fragments of PRB-RA, which covered about 70% of the deduced sequence. Northern blot hybridization of poly(A)+ RNA isolated from rat tissues showed the presence of predominant and minor mRNA species of about 2.0 and 4.3 kilobases, respectively, in the liver and kidney. A sequence homology search revealed that PRB-RA is almost completely identical to rat cystathionine gamma-lyase (cystathionase) and that it does not show overall homology with probasin. Three candidates for an epitope common to probasin and PRB-RA were found on close examination of the amino acid sequences of the two proteins. A synthetic peptide, TYFRRI, corresponding to one of the candidates, neutralized the reactivity of the anti-probasin monoclonal antibody to both probasin and PRB-RA on Western blot analysis. These results show that PRB-RA/cystathionase is neither structurally nor functionally related to probasin except for a common epitope and that cystathionase, a cystein-producing enzyme, is localized in urinary tubular epithelial cells in a highly restricted region of the kidney in addition to in liver parenchymal cells."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":162,"end":165},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":236,"end":239},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":488,"end":491},"obj":"OrganismTaxon"},{"id":"T7","span":{"begin":814,"end":817},"obj":"OrganismTaxon"},{"id":"T9","span":{"begin":1037,"end":1040},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"10114"},{"id":"A2","pred":"db_id","subj":"T1","obj":"10116"},{"id":"A3","pred":"db_id","subj":"T3","obj":"10114"},{"id":"A4","pred":"db_id","subj":"T3","obj":"10116"},{"id":"A5","pred":"db_id","subj":"T5","obj":"10114"},{"id":"A6","pred":"db_id","subj":"T5","obj":"10116"},{"id":"A7","pred":"db_id","subj":"T7","obj":"10114"},{"id":"A8","pred":"db_id","subj":"T7","obj":"10116"},{"id":"A9","pred":"db_id","subj":"T9","obj":"10114"},{"id":"A10","pred":"db_id","subj":"T9","obj":"10116"}],"text":"Identification of probasin-related antigen as cystathionine gamma-lyase by molecular cloning.\nWe reported previously that a monoclonal antibody against probasin (rat prostatic secretory protein) recognizes a 40-kDa protein localized in rat liver and kidney. The protein (probasin-related antigen, PRB-RA) may participate in a specific differentiated function of these tissues. To clarify the molecular nature of PRB-RA, a series of cDNA clones coding for the protein were isolated from a rat liver expression library using an affinity-purified polyclonal antibody. The amino acid sequence deduced from the determined cDNA sequence included sequences identical with those of proteolytic fragments of PRB-RA, which covered about 70% of the deduced sequence. Northern blot hybridization of poly(A)+ RNA isolated from rat tissues showed the presence of predominant and minor mRNA species of about 2.0 and 4.3 kilobases, respectively, in the liver and kidney. A sequence homology search revealed that PRB-RA is almost completely identical to rat cystathionine gamma-lyase (cystathionase) and that it does not show overall homology with probasin. Three candidates for an epitope common to probasin and PRB-RA were found on close examination of the amino acid sequences of the two proteins. A synthetic peptide, TYFRRI, corresponding to one of the candidates, neutralized the reactivity of the anti-probasin monoclonal antibody to both probasin and PRB-RA on Western blot analysis. These results show that PRB-RA/cystathionase is neither structurally nor functionally related to probasin except for a common epitope and that cystathionase, a cystein-producing enzyme, is localized in urinary tubular epithelial cells in a highly restricted region of the kidney in addition to in liver parenchymal cells."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":240,"end":245},"obj":"Body_part"},{"id":"T2","span":{"begin":250,"end":256},"obj":"Body_part"},{"id":"T3","span":{"begin":492,"end":497},"obj":"Body_part"},{"id":"T4","span":{"begin":937,"end":942},"obj":"Body_part"},{"id":"T5","span":{"begin":947,"end":953},"obj":"Body_part"},{"id":"T6","span":{"begin":1693,"end":1709},"obj":"Body_part"},{"id":"T7","span":{"begin":1747,"end":1753},"obj":"Body_part"},{"id":"T8","span":{"begin":1772,"end":1789},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0002107"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0002113"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0002107"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0002107"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0002113"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/CL_0000066"},{"id":"A7","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/UBERON_0002113"},{"id":"A8","pred":"uberon_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/UBERON_0001280"}],"text":"Identification of probasin-related antigen as cystathionine gamma-lyase by molecular cloning.\nWe reported previously that a monoclonal antibody against probasin (rat prostatic secretory protein) recognizes a 40-kDa protein localized in rat liver and kidney. The protein (probasin-related antigen, PRB-RA) may participate in a specific differentiated function of these tissues. To clarify the molecular nature of PRB-RA, a series of cDNA clones coding for the protein were isolated from a rat liver expression library using an affinity-purified polyclonal antibody. The amino acid sequence deduced from the determined cDNA sequence included sequences identical with those of proteolytic fragments of PRB-RA, which covered about 70% of the deduced sequence. Northern blot hybridization of poly(A)+ RNA isolated from rat tissues showed the presence of predominant and minor mRNA species of about 2.0 and 4.3 kilobases, respectively, in the liver and kidney. A sequence homology search revealed that PRB-RA is almost completely identical to rat cystathionine gamma-lyase (cystathionase) and that it does not show overall homology with probasin. Three candidates for an epitope common to probasin and PRB-RA were found on close examination of the amino acid sequences of the two proteins. A synthetic peptide, TYFRRI, corresponding to one of the candidates, neutralized the reactivity of the anti-probasin monoclonal antibody to both probasin and PRB-RA on Western blot analysis. These results show that PRB-RA/cystathionase is neither structurally nor functionally related to probasin except for a common epitope and that cystathionase, a cystein-producing enzyme, is localized in urinary tubular epithelial cells in a highly restricted region of the kidney in addition to in liver parenchymal cells."}

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":787,"end":791},"obj":"Cell"},{"id":"T3","span":{"begin":1693,"end":1709},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000096"},{"id":"A2","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000066"}],"text":"Identification of probasin-related antigen as cystathionine gamma-lyase by molecular cloning.\nWe reported previously that a monoclonal antibody against probasin (rat prostatic secretory protein) recognizes a 40-kDa protein localized in rat liver and kidney. The protein (probasin-related antigen, PRB-RA) may participate in a specific differentiated function of these tissues. To clarify the molecular nature of PRB-RA, a series of cDNA clones coding for the protein were isolated from a rat liver expression library using an affinity-purified polyclonal antibody. The amino acid sequence deduced from the determined cDNA sequence included sequences identical with those of proteolytic fragments of PRB-RA, which covered about 70% of the deduced sequence. Northern blot hybridization of poly(A)+ RNA isolated from rat tissues showed the presence of predominant and minor mRNA species of about 2.0 and 4.3 kilobases, respectively, in the liver and kidney. A sequence homology search revealed that PRB-RA is almost completely identical to rat cystathionine gamma-lyase (cystathionase) and that it does not show overall homology with probasin. Three candidates for an epitope common to probasin and PRB-RA were found on close examination of the amino acid sequences of the two proteins. A synthetic peptide, TYFRRI, corresponding to one of the candidates, neutralized the reactivity of the anti-probasin monoclonal antibody to both probasin and PRB-RA on Western blot analysis. These results show that PRB-RA/cystathionase is neither structurally nor functionally related to probasin except for a common epitope and that cystathionase, a cystein-producing enzyme, is localized in urinary tubular epithelial cells in a highly restricted region of the kidney in addition to in liver parenchymal cells."}