PMC:2726924 / 17698-18252 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/2726924","sourcedb":"PMC","sourceid":"2726924","source_url":"https://www.ncbi.nlm.nih.gov/pmc/2726924","text":"Amyloid fibril preparation\nRecombinant wild-type β2m was expressed in Escherichia coli and purified to homogeneity.26 The recombinant wild-type protein contained all 99 residues plus the N-terminal methionine, and the single disulfide bond was oxidised. Fibrils were formed by incubation of the protein (0.3–0.5 mg/ml) for 2–8 weeks at pH 2.5 in 25 mM sodium phosphate and 25 mM sodium acetate buffer containing 0.03% (wt/vol) sodium azide at 37 °C. At pH 7.0, fibrils were grown by elongation of heparin-stabilised seeds from fibrils formed at pH 2.5.24","divisions":[{"label":"title","span":{"begin":0,"end":26}}],"tracks":[{"project":"2_test","denotations":[{"id":"19345691-15663944-62520796","span":{"begin":115,"end":117},"obj":"15663944"},{"id":"19345691-16475820-62520797","span":{"begin":552,"end":554},"obj":"16475820"}],"attributes":[{"subj":"19345691-15663944-62520796","pred":"source","obj":"2_test"},{"subj":"19345691-16475820-62520797","pred":"source","obj":"2_test"}]}],"config":{"attribute types":[{"pred":"source","value type":"selection","values":[{"id":"2_test","color":"#ec93de","default":true}]}]}}