Konami Y, Yamamoto K, Osawa T, Irimura T
Department of Cancer Biology and Molecular Immunology, Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
Glycoconj J. 1995 Apr;12(2):128-34. doi: 10.1007/BF00731356.
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).
使用蛋白质测序仪测定了一种乳糖结合型无叶豆抗H（O）凝集素II（CSA-II）的完整氨基酸序列。用内肽酶Lys-C或Asp-N消化CSA-II后，所得肽段通过反相高效液相色谱（HPLC）纯化，然后进行序列分析。将CSA-II的完整氨基酸序列与其他豆科种子凝集素的序列进行比较，发现了广泛的同源区域。CSA-II假定的碳水化合物结合结构域的氨基酸序列与几种抗H（O）豆科凝集素的序列相似，尤其与L-岩藻糖结合的欧洲荆豆凝集素I（UEA-I）的序列相似。
