PubMed:811654 / 448-854
Annnotations
CL-cell
{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":120,"end":124},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000560"}],"text":"The protein isolated under nondenaturing conditions appeared to be essentially homogeneous by its migration as a single band on (a) cellulose acetate membrane electrophoresis at pH 8.6; (B) 4% and 7.5% polyacrylamide gel electrophoresis at ph 8.9; (C) sodium dodecyl sulfate (10%) polyacrylamide gel electrophoresis at pH 7.0; and by (d) its complete freedom from collagen, the major contaminating protein."}
sentences
{"project":"sentences","denotations":[{"id":"T4","span":{"begin":0,"end":406},"obj":"Sentence"},{"id":"T4","span":{"begin":0,"end":406},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"The protein isolated under nondenaturing conditions appeared to be essentially homogeneous by its migration as a single band on (a) cellulose acetate membrane electrophoresis at pH 8.6; (B) 4% and 7.5% polyacrylamide gel electrophoresis at ph 8.9; (C) sodium dodecyl sulfate (10%) polyacrylamide gel electrophoresis at pH 7.0; and by (d) its complete freedom from collagen, the major contaminating protein."}
Anatomy-UBERON
{"project":"Anatomy-UBERON","denotations":[{"id":"T9","span":{"begin":150,"end":158},"obj":"Body_part"}],"attributes":[{"id":"A9","pred":"uberon_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"A10","pred":"uberon_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/UBERON_0000094"},{"id":"A11","pred":"uberon_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/UBERON_0000158"}],"text":"The protein isolated under nondenaturing conditions appeared to be essentially homogeneous by its migration as a single band on (a) cellulose acetate membrane electrophoresis at pH 8.6; (B) 4% and 7.5% polyacrylamide gel electrophoresis at ph 8.9; (C) sodium dodecyl sulfate (10%) polyacrylamide gel electrophoresis at pH 7.0; and by (d) its complete freedom from collagen, the major contaminating protein."}