PubMed:6234315 JSON TXT

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sentences

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":95},"obj":"Sentence"},{"id":"T2","span":{"begin":96,"end":301},"obj":"Sentence"},{"id":"T3","span":{"begin":302,"end":553},"obj":"Sentence"},{"id":"T4","span":{"begin":554,"end":653},"obj":"Sentence"},{"id":"T5","span":{"begin":654,"end":819},"obj":"Sentence"},{"id":"T6","span":{"begin":820,"end":957},"obj":"Sentence"},{"id":"T7","span":{"begin":958,"end":1044},"obj":"Sentence"},{"id":"T8","span":{"begin":1045,"end":1180},"obj":"Sentence"},{"id":"T9","span":{"begin":1181,"end":1338},"obj":"Sentence"},{"id":"T10","span":{"begin":1339,"end":1451},"obj":"Sentence"},{"id":"T11","span":{"begin":1452,"end":1752},"obj":"Sentence"},{"id":"T12","span":{"begin":1753,"end":2092},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":95},"obj":"Sentence"},{"id":"T2","span":{"begin":96,"end":301},"obj":"Sentence"},{"id":"T3","span":{"begin":302,"end":553},"obj":"Sentence"},{"id":"T4","span":{"begin":554,"end":653},"obj":"Sentence"},{"id":"T5","span":{"begin":654,"end":819},"obj":"Sentence"},{"id":"T6","span":{"begin":820,"end":957},"obj":"Sentence"},{"id":"T7","span":{"begin":958,"end":1044},"obj":"Sentence"},{"id":"T8","span":{"begin":1045,"end":1180},"obj":"Sentence"},{"id":"T9","span":{"begin":1181,"end":1338},"obj":"Sentence"},{"id":"T10","span":{"begin":1339,"end":1451},"obj":"Sentence"},{"id":"T11","span":{"begin":1452,"end":1752},"obj":"Sentence"},{"id":"T12","span":{"begin":1753,"end":2092},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Complex formation of platelet membrane glycoproteins IIb and IIIa with the fibrinogen D domain.\nGlycoprotein IIb (GPIIb) and glycoprotein IIIa (GPIIIa) form a macromolecular complex on the activated platelet surface which contains the fibrinogen-binding site necessary for normal platelet aggregation. To identify the specific region of the fibrinogen molecule responsible for its interaction with the GPIIb-GPIIIa complex, purified fragment D1 (Mr = 100,000) and fragment E (Mr = 50,000) were prepared from plasmin digests of purified human fibrinogen. In addition, the polypeptide chain subunits A alpha, B beta, and gamma of fibrinogen were prepared. Using an enzyme-linked immunosorbent assay we have demonstrated that isolated fragment D1 in a solid phase system forms a complex with a mixture of GPIIb and GPIIIa. The binding of the GPIIb-GPIIIa mixture to fragment D1-coated plates reached saturation at 8 nM and to fibrinogen-coated plates at 24 nM. Isolated A alpha, B beta, and gamma chains were not reactive with added glycoproteins. Fragment E coated directly on plastic plates or immobilized on antibody-coated plastic plates did not form a complex with GPIIb-GPIIIa. Only fluid phase fibrinogen and fragment D1 but not fragment E were inhibitory toward formation of a complex between solid phase fibrinogen and GPIIb-GPIIIa. Isolated A alpha, B beta, and gamma chains at concentrations equivalent to fluid phase fibrinogen were inactive. Binding of fragment D1 but not fragment E to the GPIIb-GPIIIa complex was also demonstrated by rocket immunoelectrophoresis of the membrane glycoprotein mixture through a gel containing the individual fragments and subsequent autoradiography of the complex following exposure to 125I-anti-fibrinogen. These observations with isolated platelet membrane glycoproteins provide strong evidence that each of the D domains of the fibrinogen molecule interacts directly with the GPIIb-GPIIIa complex on the activated platelet surface, thus allowing formation of a tertiary molecular \"bridge\" across the surface of two adjacent activated platelets."}

spacy-test

NCBITAXON

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":536,"end":541},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"}],"text":"Complex formation of platelet membrane glycoproteins IIb and IIIa with the fibrinogen D domain.\nGlycoprotein IIb (GPIIb) and glycoprotein IIIa (GPIIIa) form a macromolecular complex on the activated platelet surface which contains the fibrinogen-binding site necessary for normal platelet aggregation. To identify the specific region of the fibrinogen molecule responsible for its interaction with the GPIIb-GPIIIa complex, purified fragment D1 (Mr = 100,000) and fragment E (Mr = 50,000) were prepared from plasmin digests of purified human fibrinogen. In addition, the polypeptide chain subunits A alpha, B beta, and gamma of fibrinogen were prepared. Using an enzyme-linked immunosorbent assay we have demonstrated that isolated fragment D1 in a solid phase system forms a complex with a mixture of GPIIb and GPIIIa. The binding of the GPIIb-GPIIIa mixture to fragment D1-coated plates reached saturation at 8 nM and to fibrinogen-coated plates at 24 nM. Isolated A alpha, B beta, and gamma chains were not reactive with added glycoproteins. Fragment E coated directly on plastic plates or immobilized on antibody-coated plastic plates did not form a complex with GPIIb-GPIIIa. Only fluid phase fibrinogen and fragment D1 but not fragment E were inhibitory toward formation of a complex between solid phase fibrinogen and GPIIb-GPIIIa. Isolated A alpha, B beta, and gamma chains at concentrations equivalent to fluid phase fibrinogen were inactive. Binding of fragment D1 but not fragment E to the GPIIb-GPIIIa complex was also demonstrated by rocket immunoelectrophoresis of the membrane glycoprotein mixture through a gel containing the individual fragments and subsequent autoradiography of the complex following exposure to 125I-anti-fibrinogen. These observations with isolated platelet membrane glycoproteins provide strong evidence that each of the D domains of the fibrinogen molecule interacts directly with the GPIIb-GPIIIa complex on the activated platelet surface, thus allowing formation of a tertiary molecular \"bridge\" across the surface of two adjacent activated platelets."}

Anatomy-UBERON

CL-cell

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":21,"end":29},"obj":"Cell"},{"id":"T2","span":{"begin":199,"end":207},"obj":"Cell"},{"id":"T3","span":{"begin":280,"end":288},"obj":"Cell"},{"id":"T4","span":{"begin":1786,"end":1794},"obj":"Cell"},{"id":"T5","span":{"begin":1962,"end":1970},"obj":"Cell"},{"id":"T6","span":{"begin":2082,"end":2091},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000233"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000233"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000233"},{"id":"A4","pred":"cl_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL:0000233"},{"id":"A5","pred":"cl_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL:0000233"},{"id":"A6","pred":"cl_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/CL:0000233"}],"text":"Complex formation of platelet membrane glycoproteins IIb and IIIa with the fibrinogen D domain.\nGlycoprotein IIb (GPIIb) and glycoprotein IIIa (GPIIIa) form a macromolecular complex on the activated platelet surface which contains the fibrinogen-binding site necessary for normal platelet aggregation. To identify the specific region of the fibrinogen molecule responsible for its interaction with the GPIIb-GPIIIa complex, purified fragment D1 (Mr = 100,000) and fragment E (Mr = 50,000) were prepared from plasmin digests of purified human fibrinogen. In addition, the polypeptide chain subunits A alpha, B beta, and gamma of fibrinogen were prepared. Using an enzyme-linked immunosorbent assay we have demonstrated that isolated fragment D1 in a solid phase system forms a complex with a mixture of GPIIb and GPIIIa. The binding of the GPIIb-GPIIIa mixture to fragment D1-coated plates reached saturation at 8 nM and to fibrinogen-coated plates at 24 nM. Isolated A alpha, B beta, and gamma chains were not reactive with added glycoproteins. Fragment E coated directly on plastic plates or immobilized on antibody-coated plastic plates did not form a complex with GPIIb-GPIIIa. Only fluid phase fibrinogen and fragment D1 but not fragment E were inhibitory toward formation of a complex between solid phase fibrinogen and GPIIb-GPIIIa. Isolated A alpha, B beta, and gamma chains at concentrations equivalent to fluid phase fibrinogen were inactive. Binding of fragment D1 but not fragment E to the GPIIb-GPIIIa complex was also demonstrated by rocket immunoelectrophoresis of the membrane glycoprotein mixture through a gel containing the individual fragments and subsequent autoradiography of the complex following exposure to 125I-anti-fibrinogen. These observations with isolated platelet membrane glycoproteins provide strong evidence that each of the D domains of the fibrinogen molecule interacts directly with the GPIIb-GPIIIa complex on the activated platelet surface, thus allowing formation of a tertiary molecular \"bridge\" across the surface of two adjacent activated platelets."}