| Literature DB >> 7620329 |
Y Konami1, K Yamamoto, T Osawa, T Irimura.
Abstract
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).Entities:
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Year: 1995 PMID: 7620329 DOI: 10.1007/BF00731356
Source DB: PubMed Journal: Glycoconj J ISSN: 0282-0080 Impact factor: 2.916