PMC:7795856 / 14971-15851 JSONTXT

{"project":"LitCovid-PubTator","denotations":[{"id":"269","span":{"begin":156,"end":163},"obj":"Gene"},{"id":"270","span":{"begin":286,"end":289},"obj":"Gene"},{"id":"271","span":{"begin":843,"end":846},"obj":"Gene"},{"id":"272","span":{"begin":466,"end":469},"obj":"Chemical"},{"id":"273","span":{"begin":523,"end":527},"obj":"Chemical"}],"attributes":[{"id":"A269","pred":"tao:has_database_id","subj":"269","obj":"Gene:3630"},{"id":"A270","pred":"tao:has_database_id","subj":"270","obj":"Gene:134864"},{"id":"A271","pred":"tao:has_database_id","subj":"271","obj":"Gene:134864"}],"namespaces":[{"prefix":"Tax","uri":"https://www.ncbi.nlm.nih.gov/taxonomy/"},{"prefix":"MESH","uri":"https://id.nlm.nih.gov/mesh/"},{"prefix":"Gene","uri":"https://www.ncbi.nlm.nih.gov/gene/"},{"prefix":"CVCL","uri":"https://web.expasy.org/cellosaurus/CVCL_"}],"text":"Of note, in contrast to classical approaches, which involve the use of an insoluble fusion partner, for example, an α-galactosidase fragment in the case of insulin [43], to provoke formation of inclusion bodies and protect the gene product from intracellular proteolysis, the PASylated Tα1 peptide was recovered as a soluble fusion protein, thus allowing direct purification from the cell extract without solubilization steps. Furthermore, the C-terminally attached PAS moiety was compatible with N-terminal acetylation by RimJ as confirmed by ESI-MS. Yields of our expression study at the research scale reached 15 mg purified acetylated Tα1-PAS and even 50 mg PAS-Tα1 per 1 L bacterial culture (at an optical density (OD) of 3), which surpasses the reported yield of a bacterially produced (yet probably non-acetylated and non-glycosylated) Tα1-Fc fusion protein (16 mg/L) [44]."}

{"project":"LitCovid-sentences","denotations":[{"id":"T92","span":{"begin":0,"end":426},"obj":"Sentence"},{"id":"T93","span":{"begin":427,"end":551},"obj":"Sentence"},{"id":"T94","span":{"begin":552,"end":880},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Of note, in contrast to classical approaches, which involve the use of an insoluble fusion partner, for example, an α-galactosidase fragment in the case of insulin [43], to provoke formation of inclusion bodies and protect the gene product from intracellular proteolysis, the PASylated Tα1 peptide was recovered as a soluble fusion protein, thus allowing direct purification from the cell extract without solubilization steps. Furthermore, the C-terminally attached PAS moiety was compatible with N-terminal acetylation by RimJ as confirmed by ESI-MS. Yields of our expression study at the research scale reached 15 mg purified acetylated Tα1-PAS and even 50 mg PAS-Tα1 per 1 L bacterial culture (at an optical density (OD) of 3), which surpasses the reported yield of a bacterially produced (yet probably non-acetylated and non-glycosylated) Tα1-Fc fusion protein (16 mg/L) [44]."}