Yamamoto K, Konami Y, Osawa T, Irimura T
Division of Chemical Toxicology and Immunochemistry, Faculty of Pharmaceutical Sciences, University of Tokyo.
J Biochem. 1992 Apr;111(4):436-9. doi: 10.1093/oxfordjournals.jbchem.a123775.
Peptide fragments have been obtained from L-fucose-binding anti-H(O) lectins [Lotus tetragonolobus lectin (LTA) and Ulex europeus lectin I (UEA-I)] and di-N-acetylchitobiose-binding anti-H(O) lectins [Ulex europeus lectin II (UEA-II) and Laburnum alpinum lectin I (LAA-I)] by treatment with endoproteinase Asp-N or Lys-C. The peptide fragments were fractionated by affinity chromatography on a column of Fuc-Gel for LTA and UEA-I, and on a column of N-acetyl-D-glucosamine oligomer-Sepharose for UEA-II and LAA-I. The peptides with affinity for these columns were identified by peptide sequencing. All of these retarded peptides were found to be parts of the metal-binding regions of these lectins. It is strongly suggested that these peptides represent the carbohydrate-binding and metal ion-binding sites of legume lectins, respectively.
通过用内切蛋白酶天冬氨酸-N或赖氨酸-C处理,从L-岩藻糖结合抗H(O)凝集素[百脉根凝集素(LTA)和欧洲荆豆凝集素I(UEA-I)]以及二-N-乙酰壳二糖结合抗H(O)凝集素[欧洲荆豆凝集素II(UEA-II)和高山金链花凝集素I(LAA-I)]中获得了肽片段。通过在LTA和UEA-I的Fuc-Gel柱上以及UEA-II和LAA-I的N-乙酰-D-葡糖胺寡聚物-琼脂糖柱上进行亲和色谱对肽片段进行分级分离。通过肽测序鉴定了对这些柱具有亲和力的肽段。发现所有这些滞留肽都是这些凝集素金属结合区域的一部分。强烈表明这些肽分别代表豆科植物凝集素的碳水化合物结合和金属离子结合位点。