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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Carbohydrate Sequence
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Chromatography, Affinity
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Chromatography, High Pressure Liquid
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Chromatography, Ion Exchange
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Disulfides / chemistry
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Disulfides / metabolism
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Egg Proteins / chemistry
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Egg Proteins / metabolism
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Fish Proteins / chemistry*
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Fish Proteins / isolation & purification
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Fish Proteins / metabolism
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Glycoproteins / chemistry*
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Glycoproteins / isolation & purification
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Glycoproteins / metabolism
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Glycosylation
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Hemagglutinins / chemistry*
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Hemagglutinins / isolation & purification
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Hemagglutinins / metabolism
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Lectins / chemistry*
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Lectins / isolation & purification
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Lectins / metabolism
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Molecular Sequence Data
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Ovum / chemistry*
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Perciformes / metabolism*
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Protein Conformation
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Protein Processing, Post-Translational*
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Protein Subunits
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Sequence Alignment
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Sequence Analysis, Protein
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Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Substances
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Disulfides
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Egg Proteins
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Fish Proteins
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Glycoproteins
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Hemagglutinins
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Lectins
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Protein Subunits