| http://purl.uniprot.org/citations/1586156 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/1586156 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/1586156 | http://www.w3.org/2000/01/rdf-schema#comment | "The cyanogenic beta-glucosidase (linamarase) of cassava is responsible for the first step in the sequential break-down of two related cyanoglucosides. Hydrolysis of these cyanoglucosides occurs following tissue damage and leads to the production of hydrocyanic acid. This mechanism is widely regarded as a defense mechanism against predation. A linamarase cDNA clone (pCAS5) was isolated from a cotyledon cDNA library using a white clover beta-glucosidase heterologous probe. The nucleotide and derived amino acid sequence is reported and five putative N-asparagine glycosylation sites are identified. Concanavalin A affinity chromatography and endoglycosidase H digestion demonstrate that linamarase from cassava is glycosylated, having high-mannose-type N-asparagine-linked oligosaccharides. Consistent with this structure and the extracellular location of the active enzyme is the identification of an N-terminal signal peptide on the deduced amino acid sequence of pCAS5."xsd:string |
| http://purl.uniprot.org/citations/1586156 | http://purl.org/dc/terms/identifier | "doi:10.1016/0003-9861(92)90518-2"xsd:string |
| http://purl.uniprot.org/citations/1586156 | http://purl.org/dc/terms/identifier | "doi:10.1016/0003-9861(92)90518-2"xsd:string |
| http://purl.uniprot.org/citations/1586156 | http://purl.uniprot.org/core/author | "Brown K."xsd:string |
| http://purl.uniprot.org/citations/1586156 | http://purl.uniprot.org/core/author | "Brown K."xsd:string |
| http://purl.uniprot.org/citations/1586156 | http://purl.uniprot.org/core/author | "Hughes J."xsd:string |
| http://purl.uniprot.org/citations/1586156 | http://purl.uniprot.org/core/author | "Hughes J."xsd:string |
| http://purl.uniprot.org/citations/1586156 | http://purl.uniprot.org/core/author | "Hughes M.A."xsd:string |
| http://purl.uniprot.org/citations/1586156 | http://purl.uniprot.org/core/author | "Hughes M.A."xsd:string |
| http://purl.uniprot.org/citations/1586156 | http://purl.uniprot.org/core/author | "Oxtoby E."xsd:string |
| http://purl.uniprot.org/citations/1586156 | http://purl.uniprot.org/core/author | "Oxtoby E."xsd:string |
| http://purl.uniprot.org/citations/1586156 | http://purl.uniprot.org/core/author | "Pancoro A."xsd:string |
| http://purl.uniprot.org/citations/1586156 | http://purl.uniprot.org/core/author | "Pancoro A."xsd:string |
| http://purl.uniprot.org/citations/1586156 | http://purl.uniprot.org/core/author | "Murray B.S."xsd:string |
| http://purl.uniprot.org/citations/1586156 | http://purl.uniprot.org/core/author | "Murray B.S."xsd:string |
| http://purl.uniprot.org/citations/1586156 | http://purl.uniprot.org/core/date | "1992"xsd:gYear |
| http://purl.uniprot.org/citations/1586156 | http://purl.uniprot.org/core/date | "1992"xsd:gYear |
| http://purl.uniprot.org/citations/1586156 | http://purl.uniprot.org/core/name | "Arch. Biochem. Biophys."xsd:string |
| http://purl.uniprot.org/citations/1586156 | http://purl.uniprot.org/core/name | "Arch Biochem Biophys"xsd:string |
| http://purl.uniprot.org/citations/1586156 | http://purl.uniprot.org/core/pages | "273-279"xsd:string |
| http://purl.uniprot.org/citations/1586156 | http://purl.uniprot.org/core/pages | "273-279"xsd:string |
| http://purl.uniprot.org/citations/1586156 | http://purl.uniprot.org/core/title | "A molecular and biochemical analysis of the structure of the cyanogenic beta-glucosidase (linamarase) from cassava (Manihot esculenta Cranz)."xsd:string |
| http://purl.uniprot.org/citations/1586156 | http://purl.uniprot.org/core/title | "A molecular and biochemical analysis of the structure of the cyanogenic beta-glucosidase (linamarase) from cassava (Manihot esculenta Cranz)."xsd:string |