Yamamoto K, Konami Y, Kusui K, Osawa T
Division of Chemical Toxicology and Immunochemistry, Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
FEBS Lett. 1991 Apr 9;281(1-2):258-62. doi: 10.1016/0014-5793(91)80406-s.
In order to examine the correlation between the amino acid sequence and sugar binding specificity of Bauhinia purpurea lectin (BPA), a galactose and lactose binding lectin, a peptide which interacts with lactose was purified from an Asp-N endoproteinase digest of BPA by means of affinity chromatography on a column of lactose-Sepharose. The amino acid sequence of this peptide is Asp-Thr-Trp-Pro-Asn-Thr-Glu-Trp-Ser. A tryptic fragment having the ability to interact with lactose was also purified and found to contain the above sequence, consisting of 9 amino acids. The chemical synthesis of this peptide was carried out by the solid-phase method and the synthetic peptide was found to exhibit lactose binding activity in the presence of calcium.
为了研究紫羊蹄甲凝集素（BPA，一种半乳糖和乳糖结合凝集素）的氨基酸序列与糖结合特异性之间的相关性，通过在乳糖-琼脂糖柱上进行亲和色谱，从BPA的天冬氨酸-N端蛋白酶消化物中纯化出一种与乳糖相互作用的肽。该肽的氨基酸序列为天冬氨酸-苏氨酸-色氨酸-脯氨酸-天冬酰胺-苏氨酸-谷氨酸-色氨酸-丝氨酸。还纯化了一个具有与乳糖相互作用能力的胰蛋白酶片段，发现其包含上述由9个氨基酸组成的序列。通过固相法进行了该肽的化学合成，并且发现合成肽在有钙存在的情况下表现出乳糖结合活性。
