PubMed:3496119 / 1163-1541 JSONTXT

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T6","span":{"begin":152,"end":159},"obj":"Glycan"},{"id":"T7","span":{"begin":333,"end":340},"obj":"Glycan"}],"attributes":[{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"https://glycosmos.org/glycans/show/G44653LT"},{"id":"A13","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G44653LT"},{"id":"A7","pred":"glycosmos_id","subj":"T7","obj":"https://glycosmos.org/glycans/show/G05740LL"},{"id":"A14","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G05740LL"}],"text":"A method is proposed based on certain properties of porcine pancreatic alpha-amylase, especially the non-interaction of the p-nitrophenyl moiety of the maltose derivative with subsites 1 and 2, and the o-nitrophenyl group which interacts in a similar way to a glucose residue at the reducing end, and on the grounds that the amylase-amylose complexes are of the productive type."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T8","span":{"begin":0,"end":378},"obj":"Sentence"}],"text":"A method is proposed based on certain properties of porcine pancreatic alpha-amylase, especially the non-interaction of the p-nitrophenyl moiety of the maltose derivative with subsites 1 and 2, and the o-nitrophenyl group which interacts in a similar way to a glucose residue at the reducing end, and on the grounds that the amylase-amylose complexes are of the productive type."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T6","span":{"begin":152,"end":159},"obj":"Glycan"},{"id":"T7","span":{"begin":333,"end":340},"obj":"Glycan"}],"attributes":[{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"https://glycosmos.org/glycans/show/G44653LT"},{"id":"A13","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G44653LT"},{"id":"A7","pred":"glycosmos_id","subj":"T7","obj":"https://glycosmos.org/glycans/show/G05740LL"},{"id":"A14","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G05740LL"}],"text":"A method is proposed based on certain properties of porcine pancreatic alpha-amylase, especially the non-interaction of the p-nitrophenyl moiety of the maltose derivative with subsites 1 and 2, and the o-nitrophenyl group which interacts in a similar way to a glucose residue at the reducing end, and on the grounds that the amylase-amylose complexes are of the productive type."}