title: Structural characterization of a rhamnose-binding glycoprotein (lectin) from Spanish mackerel (Scomberomorous niphonius) eggs.
abstract: A rhamnose-binding glycoprotein (lectin), named SML, was isolated from the eggs of Spanish mackerel (Scomberomorous niphonius) by affinity and ion-exchange chromatographies. SML was composed of a non-covalently linked homodimer. The SML subunit was composed of 201 amino acid residues with two tandemly repeated domains, and contained 8 half-Cys residues in each domain, which is highly homologous to the N-terminal lectin domain of calcium-independent alpha-latrotoxin receptor in mammalian brains. Each domain has the same disulfide bonding pattern; Cys10-Cys40, Cys20-Cys99, Cys54-Cys86 and Cys67-Cys73 were located in the N-terminal domain, and Cys108-Cys138, Cys117-Cys195, Cys152-Cys182 and Cys163-Cys169 were in the C-terminal domain. SML was N-glycosylated at Asn168 in the C-terminal domain. The structure of the sugar chain was determined to be NeuAc-Galbeta1-4GlcNAcbeta1-2Manalpha1-6-(NeuAc-Galbeta1-4GlcNAcbeta1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-4GlcNAc-Asn.
authors.affiliation: Department of Biomolecular Science, Graduate School of Life Sciences, Tohoku University, Sendai 981-8555, Japan.
authors.forename: Takatomo
authors.initials: T
authors.lastname: Terada
authors.forename: Yasuharu
authors.initials: Y
authors.lastname: Watanabe
authors.forename: Hiroaki
authors.initials: H
authors.lastname: Tateno
authors.forename: Takako
authors.initials: T
authors.lastname: Naganuma
authors.forename: Tomohisa
authors.initials: T
authors.lastname: Ogawa
authors.forename: Koji
authors.initials: K
authors.lastname: Muramoto
authors.forename: Hisao
authors.initials: H
authors.lastname: Kamiya
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002240:Carbohydrate Sequence; D002846:Chromatography, Affinity; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D004220:Disulfides / Q000737:chemistry / Q000378:metabolism; D004527:Egg Proteins / Q000737:chemistry / Q000378:metabolism; D029941:Fish Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D006023:Glycoproteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D006031:Glycosylation; D006388:Hemagglutinins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D037102:Lectins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D008969:Molecular Sequence Data; D010063:Ovum / Q000737:chemistry*; D010473:Perciformes / Q000378:metabolism*; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D021122:Protein Subunits; D016415:Sequence Alignment; D020539:Sequence Analysis, Protein; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D004220:Disulfides; D004527:Egg Proteins; D029941:Fish Proteins; D006023:Glycoproteins; D006388:Hemagglutinins; D037102:Lectins; D021122:Protein Subunits