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http://purl.uniprot.org/citations/27720757http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27720757http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27720757http://www.w3.org/2000/01/rdf-schema#comment"Seeds of Maackia amurensis constitutes two sialic acid specific agglutinins known as leukagglutinin and hemagglutinin. Maackia amurensis leukagglutinin (MAL) recognizes α2-3-linked sialic acid present mainly in N-glycans and composed of two disulfide linked monomers. It exhibits potential N-glycosylation sites (four PNGs) which have been assumed to undergo differential occupancy. In this study we have characterized the site specific macro- and microheterogeneity of monomers in detail by analysing N-glycopeptides and peptides through liquid chromatography coupled to ion trap mass spectrometer in MS3 mode (LC-MSn). We observed the presence of mainly paucimannose N-glycans at Asn61, Asn113 and Asn191 whereas a high mannose type with varying Man5-9 occurs at Asn179. Interestingly Asn179 and Asn191 exhibited differential occupancy which was evident by the presence of non-glycosylated peptides. This has contributed to the difference in molecular mass of monomers upon SDS-PAGE. Further the presence of disulfide linked peptides confirmed the covalent linkage of monomers which also undergoes uniform C-terminal processing."xsd:string
http://purl.uniprot.org/citations/27720757http://purl.org/dc/terms/identifier"doi:10.1016/j.ijbiomac.2016.10.007"xsd:string
http://purl.uniprot.org/citations/27720757http://purl.org/dc/terms/identifier"doi:10.1016/j.ijbiomac.2016.10.007"xsd:string
http://purl.uniprot.org/citations/27720757http://purl.uniprot.org/core/author"Surolia A."xsd:string
http://purl.uniprot.org/citations/27720757http://purl.uniprot.org/core/author"Surolia A."xsd:string
http://purl.uniprot.org/citations/27720757http://purl.uniprot.org/core/author"Gnanesh Kumar B.S."xsd:string
http://purl.uniprot.org/citations/27720757http://purl.uniprot.org/core/author"Gnanesh Kumar B.S."xsd:string
http://purl.uniprot.org/citations/27720757http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/27720757http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/27720757http://purl.uniprot.org/core/name"Int. J. Biol. Macromol."xsd:string
http://purl.uniprot.org/citations/27720757http://purl.uniprot.org/core/name"Int. J. Biol. Macromol."xsd:string
http://purl.uniprot.org/citations/27720757http://purl.uniprot.org/core/pages"114-121"xsd:string
http://purl.uniprot.org/citations/27720757http://purl.uniprot.org/core/pages"114-121"xsd:string
http://purl.uniprot.org/citations/27720757http://purl.uniprot.org/core/title"Comprehensive analysis of alpha 2-3-linked sialic acid specific Maackia amurensis leukagglutinin reveals differentially occupied N-glycans and C-terminal processing."xsd:string
http://purl.uniprot.org/citations/27720757http://purl.uniprot.org/core/title"Comprehensive analysis of alpha 2-3-linked sialic acid specific Maackia amurensis leukagglutinin reveals differentially occupied N-glycans and C-terminal processing."xsd:string
http://purl.uniprot.org/citations/27720757http://purl.uniprot.org/core/volume"94"xsd:string
http://purl.uniprot.org/citations/27720757http://purl.uniprot.org/core/volume"94"xsd:string
http://purl.uniprot.org/citations/27720757http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/27720757
http://purl.uniprot.org/citations/27720757http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/27720757
http://purl.uniprot.org/citations/27720757http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/27720757
http://purl.uniprot.org/citations/27720757http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/27720757
http://purl.uniprot.org/uniprot/P0DKL3http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/27720757
http://purl.uniprot.org/uniprot/P0DKL3#attribution-E246538D482737D510F83B34527C616Ahttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/27720757