Abstract
The complete amino acid sequence of a lactose-bindingCytisus 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 thel-fucose-bindingUlex europaeus lectin I (UEA-I).
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Abbreviations
- BPA:
-
Bauhinia purpurea lectin
- Con A:
-
concanavalin A
- CMA-I:
-
Cytisus multiflorus lectin I
- CMA-II:
-
Cytisus multiflorus lectin II
- CSA-I:
-
Cytisus sessilifolius lectin I
- CSA-II:
-
Cytisus sessilifolius lectin II
- CSII:
-
Cytisus scoparius lectin II
- ECorL:
-
Erythrina corallodendron lectin
- GSIV:
-
Griffonia simplicifolia lectin IV
- HPLC:
-
high performance liquid chromatography
- LAA-I:
-
Laburnum alpinum lectin I
- LAA-II:
-
Laburnum alpinum lectin II
- LOL:
-
Lathyrus ochrus lectin
- LTA:
-
Lotus tetragonolobus lectin
- MAH:
-
Maackia amurensis haemagglutinin
- PSA:
-
Pisum sativum lectin
- SDS:
-
sodium dodecyl sulfate
- TFA:
-
trifluoroacetic acid
- UEA-I:
-
Ulex europaeus lectin I
- UEA-II:
-
Ulex europaeus lectin II
- VFA:
-
Vicia faba lectin
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Konami, Y., Yamamoto, K., Osawa, T. et al. A putative carbohydrate-binding domain of the lactosebindingCytisus sessilifolius anti-H(O) lectin has a similar amino acid sequence to that of thel-fucose-bindingUlex europaeus anti-H(O) lectin. Glycoconjugate J 12, 128–134 (1995). https://doi.org/10.1007/BF00731356
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DOI: https://doi.org/10.1007/BF00731356