A putative carbohydrate-binding domain of the lactose-binding Cytisus sessilifolius anti-H(O) lectin has a similar amino acid sequence to that of the L-fucose-binding Ulex europaeus anti-H(O) lectin.
The complete amino acid sequence of a lactose-binding Cytisus sessilifolius anti-H(O) lectin II (CSA-II) was determined using a protein sequencer. After digestion of CSA-II with endoproteinase Lys-C or Asp-N, the resulting peptides were purified by reversed-phase high performance liquid chromatography (HPLC) and then subjected to sequence analysis. Comparison of the complete amino acid sequence of CSA-II with the sequences of other leguminous seed lectins revealed regions of extensive homology. The amino acid sequence of a putative carbohydrate-binding domain of CSA-II was found to be similar to those of several anti-H(O) leguminous lectins, especially to that of the L-fucose-binding Ulex europaeus lectin I (UEA-I).
Konami
Y
Y
Department of Cancer Biology and Molecular Immunology, Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
Yamamoto
K
K
Osawa
T
T
Irimura
T
T
D000595:Amino Acid Sequence; D001665:Binding Sites; D010450:Endopeptidases / Q000378:metabolism; D007887:Fabaceae; D005643:Fucose / Q000378:metabolism; D007785:Lactose / Q000378:metabolism*; D037102:Lectins / Q000737:chemistry*; D008666:Metalloendopeptidases / Q000378:metabolism; D008969:Molecular Sequence Data; D008970:Molecular Weight; D037121:Plant Lectins; D010946:Plants, Medicinal; D012639:Seeds / Q000737:chemistry*; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid
C075400:Cytisus-type anti-H(O) lectins; D037102:Lectins; D037121:Plant Lectins; C036850:Ulex europaeus lectins; D005643:Fucose; D010450:Endopeptidases; D008666:Metalloendopeptidases; C039830:peptidyl-Lys metalloendopeptidase; C058921:endoproteinase Asp-N; D007785:Lactose