PMC:3317373 / 10541-11434 JSON TXT

Annnotations TAB JSON ListView MergeView

pmc-enju-pas

bionlp-st-ge-2016-test-proteins

{"project":"bionlp-st-ge-2016-test-proteins","denotations":[{"id":"T4389","span":{"begin":826,"end":830},"obj":"Protein"},{"id":"T4388","span":{"begin":570,"end":574},"obj":"Protein"}],"namespaces":[{"prefix":"_base","uri":"http://bionlp.dbcls.jp/ontology/ge.owl#"}],"text":"2.8. Gelatine Zymography\nCells of four groups were homogenized in lysis buffer containing 50 mM Tris-HCl (pH 7.4), 150 mM NaCl, 5 mM CaCl2, 0.2 mM NaN3, and 0.01% Triton. Soluble extracts were separated by centrifugation and stored at –20°C. Gelatin zymography was performed according to the manufacturer's instructions (Genmed Scientifics Inc, MA, USA). Briefly, 40 μg cytosolic protein extracts were separated by electrophoresis. Then the proteins were renatured by incubation in 2.5% Triton X-100 and then incubated in substrate buffer for 40 h at 37°C to enable the MMP9 to cleave the gelatin. After rinsing in water, each gel was stained with Coomassie blue for 1 h and destained in 50% methanol. Proteolytic activities were showed by clear bands in blue gel which indicates the lysis of the substrate. Quantification of MMP9 band density was performed with image analysis program ImageJ."}

GO-BP

{"project":"GO-BP","denotations":[{"id":"T4391","span":{"begin":784,"end":789},"obj":"http://purl.obolibrary.org/obo/GO_0019835"},{"id":"T4390","span":{"begin":66,"end":71},"obj":"http://purl.obolibrary.org/obo/GO_0019835"}],"text":"2.8. Gelatine Zymography\nCells of four groups were homogenized in lysis buffer containing 50 mM Tris-HCl (pH 7.4), 150 mM NaCl, 5 mM CaCl2, 0.2 mM NaN3, and 0.01% Triton. Soluble extracts were separated by centrifugation and stored at –20°C. Gelatin zymography was performed according to the manufacturer's instructions (Genmed Scientifics Inc, MA, USA). Briefly, 40 μg cytosolic protein extracts were separated by electrophoresis. Then the proteins were renatured by incubation in 2.5% Triton X-100 and then incubated in substrate buffer for 40 h at 37°C to enable the MMP9 to cleave the gelatin. After rinsing in water, each gel was stained with Coomassie blue for 1 h and destained in 50% methanol. Proteolytic activities were showed by clear bands in blue gel which indicates the lysis of the substrate. Quantification of MMP9 band density was performed with image analysis program ImageJ."}

sentences

{"project":"sentences","denotations":[{"id":"T4385","span":{"begin":808,"end":893},"obj":"Sentence"},{"id":"T4384","span":{"begin":702,"end":807},"obj":"Sentence"},{"id":"T4383","span":{"begin":598,"end":701},"obj":"Sentence"},{"id":"T4382","span":{"begin":432,"end":597},"obj":"Sentence"},{"id":"T4381","span":{"begin":355,"end":431},"obj":"Sentence"},{"id":"T4380","span":{"begin":25,"end":354},"obj":"Sentence"},{"id":"T4379","span":{"begin":5,"end":24},"obj":"Sentence"},{"id":"T4378","span":{"begin":0,"end":4},"obj":"Sentence"},{"id":"T107","span":{"begin":0,"end":4},"obj":"Sentence"},{"id":"T108","span":{"begin":5,"end":24},"obj":"Sentence"},{"id":"T109","span":{"begin":25,"end":170},"obj":"Sentence"},{"id":"T110","span":{"begin":171,"end":241},"obj":"Sentence"},{"id":"T111","span":{"begin":242,"end":354},"obj":"Sentence"},{"id":"T112","span":{"begin":355,"end":431},"obj":"Sentence"},{"id":"T113","span":{"begin":432,"end":597},"obj":"Sentence"},{"id":"T114","span":{"begin":598,"end":701},"obj":"Sentence"},{"id":"T115","span":{"begin":702,"end":807},"obj":"Sentence"},{"id":"T116","span":{"begin":808,"end":893},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"2.8. Gelatine Zymography\nCells of four groups were homogenized in lysis buffer containing 50 mM Tris-HCl (pH 7.4), 150 mM NaCl, 5 mM CaCl2, 0.2 mM NaN3, and 0.01% Triton. Soluble extracts were separated by centrifugation and stored at –20°C. Gelatin zymography was performed according to the manufacturer's instructions (Genmed Scientifics Inc, MA, USA). Briefly, 40 μg cytosolic protein extracts were separated by electrophoresis. Then the proteins were renatured by incubation in 2.5% Triton X-100 and then incubated in substrate buffer for 40 h at 37°C to enable the MMP9 to cleave the gelatin. After rinsing in water, each gel was stained with Coomassie blue for 1 h and destained in 50% methanol. Proteolytic activities were showed by clear bands in blue gel which indicates the lysis of the substrate. Quantification of MMP9 band density was performed with image analysis program ImageJ."}

simple1

{"project":"simple1","denotations":[{"id":"T4551","span":{"begin":826,"end":830},"obj":"Protein"},{"id":"T4550","span":{"begin":570,"end":574},"obj":"Protein"}],"text":"2.8. Gelatine Zymography\nCells of four groups were homogenized in lysis buffer containing 50 mM Tris-HCl (pH 7.4), 150 mM NaCl, 5 mM CaCl2, 0.2 mM NaN3, and 0.01% Triton. Soluble extracts were separated by centrifugation and stored at –20°C. Gelatin zymography was performed according to the manufacturer's instructions (Genmed Scientifics Inc, MA, USA). Briefly, 40 μg cytosolic protein extracts were separated by electrophoresis. Then the proteins were renatured by incubation in 2.5% Triton X-100 and then incubated in substrate buffer for 40 h at 37°C to enable the MMP9 to cleave the gelatin. After rinsing in water, each gel was stained with Coomassie blue for 1 h and destained in 50% methanol. Proteolytic activities were showed by clear bands in blue gel which indicates the lysis of the substrate. Quantification of MMP9 band density was performed with image analysis program ImageJ."}

BioNLP16_DUT

{"project":"BioNLP16_DUT","denotations":[{"id":"T4732","span":{"begin":826,"end":830},"obj":"Protein"},{"id":"T4731","span":{"begin":570,"end":574},"obj":"Protein"}],"text":"2.8. Gelatine Zymography\nCells of four groups were homogenized in lysis buffer containing 50 mM Tris-HCl (pH 7.4), 150 mM NaCl, 5 mM CaCl2, 0.2 mM NaN3, and 0.01% Triton. Soluble extracts were separated by centrifugation and stored at –20°C. Gelatin zymography was performed according to the manufacturer's instructions (Genmed Scientifics Inc, MA, USA). Briefly, 40 μg cytosolic protein extracts were separated by electrophoresis. Then the proteins were renatured by incubation in 2.5% Triton X-100 and then incubated in substrate buffer for 40 h at 37°C to enable the MMP9 to cleave the gelatin. After rinsing in water, each gel was stained with Coomassie blue for 1 h and destained in 50% methanol. Proteolytic activities were showed by clear bands in blue gel which indicates the lysis of the substrate. Quantification of MMP9 band density was performed with image analysis program ImageJ."}

BioNLP16_Messiy

{"project":"BioNLP16_Messiy","denotations":[{"id":"T4556","span":{"begin":578,"end":584},"obj":"Protein_catabolism"},{"id":"T4555","span":{"begin":826,"end":830},"obj":"Protein"},{"id":"T4554","span":{"begin":570,"end":574},"obj":"Protein"}],"relations":[{"id":"R3872","pred":"themeOf","subj":"T4554","obj":"T4556"}],"text":"2.8. Gelatine Zymography\nCells of four groups were homogenized in lysis buffer containing 50 mM Tris-HCl (pH 7.4), 150 mM NaCl, 5 mM CaCl2, 0.2 mM NaN3, and 0.01% Triton. Soluble extracts were separated by centrifugation and stored at –20°C. Gelatin zymography was performed according to the manufacturer's instructions (Genmed Scientifics Inc, MA, USA). Briefly, 40 μg cytosolic protein extracts were separated by electrophoresis. Then the proteins were renatured by incubation in 2.5% Triton X-100 and then incubated in substrate buffer for 40 h at 37°C to enable the MMP9 to cleave the gelatin. After rinsing in water, each gel was stained with Coomassie blue for 1 h and destained in 50% methanol. Proteolytic activities were showed by clear bands in blue gel which indicates the lysis of the substrate. Quantification of MMP9 band density was performed with image analysis program ImageJ."}

DLUT931

{"project":"DLUT931","denotations":[{"id":"T4553","span":{"begin":826,"end":830},"obj":"Protein"},{"id":"T4552","span":{"begin":570,"end":574},"obj":"Protein"}],"text":"2.8. Gelatine Zymography\nCells of four groups were homogenized in lysis buffer containing 50 mM Tris-HCl (pH 7.4), 150 mM NaCl, 5 mM CaCl2, 0.2 mM NaN3, and 0.01% Triton. Soluble extracts were separated by centrifugation and stored at –20°C. Gelatin zymography was performed according to the manufacturer's instructions (Genmed Scientifics Inc, MA, USA). Briefly, 40 μg cytosolic protein extracts were separated by electrophoresis. Then the proteins were renatured by incubation in 2.5% Triton X-100 and then incubated in substrate buffer for 40 h at 37°C to enable the MMP9 to cleave the gelatin. After rinsing in water, each gel was stained with Coomassie blue for 1 h and destained in 50% methanol. Proteolytic activities were showed by clear bands in blue gel which indicates the lysis of the substrate. Quantification of MMP9 band density was performed with image analysis program ImageJ."}

bionlp-st-ge-2016-test-ihmc

{"project":"bionlp-st-ge-2016-test-ihmc","denotations":[{"id":"T4752","span":{"begin":5,"end":13},"obj":"Entity"},{"id":"T4751","span":{"begin":522,"end":531},"obj":"Entity"},{"id":"T4750","span":{"begin":364,"end":396},"obj":"Entity"},{"id":"T4749","span":{"begin":25,"end":45},"obj":"Entity"},{"id":"T4748","span":{"begin":667,"end":670},"obj":"Entity"},{"id":"T4747","span":{"begin":482,"end":499},"obj":"Entity"},{"id":"T4746","span":{"begin":171,"end":187},"obj":"Entity"},{"id":"T4745","span":{"begin":566,"end":574},"obj":"Protein"},{"id":"T4744","span":{"begin":140,"end":169},"obj":"Entity"},{"id":"T4743","span":{"begin":157,"end":169},"obj":"Entity"},{"id":"T4742","span":{"begin":90,"end":104},"obj":"Entity"},{"id":"T4741","span":{"begin":755,"end":806},"obj":"Entity"},{"id":"T4740","span":{"begin":115,"end":126},"obj":"Entity"},{"id":"T4739","span":{"begin":622,"end":630},"obj":"Entity"},{"id":"T4738","span":{"begin":826,"end":830},"obj":"Protein"},{"id":"T4737","span":{"begin":364,"end":396},"obj":"Protein"},{"id":"T4736","span":{"begin":242,"end":249},"obj":"Entity"},{"id":"T4735","span":{"begin":437,"end":449},"obj":"Protein"},{"id":"T4734","span":{"begin":90,"end":104},"obj":"Entity"},{"id":"T4733","span":{"begin":688,"end":700},"obj":"Entity"}],"text":"2.8. Gelatine Zymography\nCells of four groups were homogenized in lysis buffer containing 50 mM Tris-HCl (pH 7.4), 150 mM NaCl, 5 mM CaCl2, 0.2 mM NaN3, and 0.01% Triton. Soluble extracts were separated by centrifugation and stored at –20°C. Gelatin zymography was performed according to the manufacturer's instructions (Genmed Scientifics Inc, MA, USA). Briefly, 40 μg cytosolic protein extracts were separated by electrophoresis. Then the proteins were renatured by incubation in 2.5% Triton X-100 and then incubated in substrate buffer for 40 h at 37°C to enable the MMP9 to cleave the gelatin. After rinsing in water, each gel was stained with Coomassie blue for 1 h and destained in 50% methanol. Proteolytic activities were showed by clear bands in blue gel which indicates the lysis of the substrate. Quantification of MMP9 band density was performed with image analysis program ImageJ."}

bionlp-st-ge-2016-spacy-parsed

bionlp-st-ge-2016-test-tees

{"project":"bionlp-st-ge-2016-test-tees","denotations":[{"id":"T4559","span":{"begin":570,"end":574},"obj":"Protein"}],"text":"2.8. Gelatine Zymography\nCells of four groups were homogenized in lysis buffer containing 50 mM Tris-HCl (pH 7.4), 150 mM NaCl, 5 mM CaCl2, 0.2 mM NaN3, and 0.01% Triton. Soluble extracts were separated by centrifugation and stored at –20°C. Gelatin zymography was performed according to the manufacturer's instructions (Genmed Scientifics Inc, MA, USA). Briefly, 40 μg cytosolic protein extracts were separated by electrophoresis. Then the proteins were renatured by incubation in 2.5% Triton X-100 and then incubated in substrate buffer for 40 h at 37°C to enable the MMP9 to cleave the gelatin. After rinsing in water, each gel was stained with Coomassie blue for 1 h and destained in 50% methanol. Proteolytic activities were showed by clear bands in blue gel which indicates the lysis of the substrate. Quantification of MMP9 band density was performed with image analysis program ImageJ."}

testone

{"project":"testone","denotations":[{"id":"T4373","span":{"begin":826,"end":830},"obj":"Protein"},{"id":"T4372","span":{"begin":570,"end":574},"obj":"Protein"}],"text":"2.8. Gelatine Zymography\nCells of four groups were homogenized in lysis buffer containing 50 mM Tris-HCl (pH 7.4), 150 mM NaCl, 5 mM CaCl2, 0.2 mM NaN3, and 0.01% Triton. Soluble extracts were separated by centrifugation and stored at –20°C. Gelatin zymography was performed according to the manufacturer's instructions (Genmed Scientifics Inc, MA, USA). Briefly, 40 μg cytosolic protein extracts were separated by electrophoresis. Then the proteins were renatured by incubation in 2.5% Triton X-100 and then incubated in substrate buffer for 40 h at 37°C to enable the MMP9 to cleave the gelatin. After rinsing in water, each gel was stained with Coomassie blue for 1 h and destained in 50% methanol. Proteolytic activities were showed by clear bands in blue gel which indicates the lysis of the substrate. Quantification of MMP9 band density was performed with image analysis program ImageJ."}

test3

{"project":"test3","denotations":[{"id":"T4377","span":{"begin":826,"end":830},"obj":"Protein"},{"id":"T4376","span":{"begin":570,"end":574},"obj":"Protein"},{"id":"T4375","span":{"begin":826,"end":830},"obj":"Protein"},{"id":"T4374","span":{"begin":570,"end":574},"obj":"Protein"}],"text":"2.8. Gelatine Zymography\nCells of four groups were homogenized in lysis buffer containing 50 mM Tris-HCl (pH 7.4), 150 mM NaCl, 5 mM CaCl2, 0.2 mM NaN3, and 0.01% Triton. Soluble extracts were separated by centrifugation and stored at –20°C. Gelatin zymography was performed according to the manufacturer's instructions (Genmed Scientifics Inc, MA, USA). Briefly, 40 μg cytosolic protein extracts were separated by electrophoresis. Then the proteins were renatured by incubation in 2.5% Triton X-100 and then incubated in substrate buffer for 40 h at 37°C to enable the MMP9 to cleave the gelatin. After rinsing in water, each gel was stained with Coomassie blue for 1 h and destained in 50% methanol. Proteolytic activities were showed by clear bands in blue gel which indicates the lysis of the substrate. Quantification of MMP9 band density was performed with image analysis program ImageJ."}

PMC:3317373 / 10541-11434 JSONTXT

Annnotations TAB JSON ListView MergeView

PMC:3317373 / 10541-11434 JSON TXT