The primary structures of two types of the Ulex europeus seed lectin.
The complete amino acid sequences of the Ulex europeus anti-H(O) lectins I and II were determined by using a protein sequencer. After digestion with endoproteinases Lys-C and Asp-N of the lectins reduced with 2-mercaptoethanol and modified with iodoacetamide, the resulting peptides were purified by reversed-phase high-performance liquid chromatography and subjected to sequence analysis. The complete primary structures of these two Ulex lectins I and II were compared with those of nine lectins already determined, including that of Lotus tetragonolobus anti-H(O) lectin which we have determined. Extensive homologies were found among them.
Konami
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Y
Division of Chemical Toxicology and Immunochemistry, Faculty of Pharmaceutical Sciences, University of Tokyo.
Yamamoto
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K
Osawa
T
T
D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D010450:Endopeptidases; D007202:Indicators and Reagents; D037102:Lectins / Q000737:chemistry* / Q000302:isolation & purification; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D037121:Plant Lectins; D012689:Sequence Homology, Nucleic Acid
D007202:Indicators and Reagents; D037102:Lectins; D010446:Peptide Fragments; D037121:Plant Lectins; C036850:Ulex europaeus lectins; D010450:Endopeptidases