Purification and characterization of a carbohydrate‐binding peptide from Bauhinia purpurea lectin
Purification and characterization of a carbohydrate‐binding peptide from Bauhinia purpurea lectin
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紫荆花凝集素中碳水化合物结合肽的纯化和表征
DOI：
10.1016/0014-5793(91)80406-s
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发表时间：
1991
期刊：
影响因子：
3.5
通讯作者：
T. Osawa
中科院分区：
文献类型：
--
作者：
Kazuo Yamamoto;Y. Konami;K. Kusui;T. Osawa
为了研究羊蹄甲凝集素（Bauhinia purpurealectin，BPA）的氨基酸序列与其糖结合特异性之间的关系，用Asp-N内切蛋白酶酶解BPA，经lactose-Sepharose柱亲和层析，得到一个与乳糖相互作用的肽段。该肽的氨基酸序列为Asp-Thr-Trp-Pro-Asn-Thr-Glu-Trp-Ser。还纯化了具有与乳糖相互作用能力的胰蛋白酶片段，发现其含有上述序列，由9个氨基酸组成。该肽的化学合成通过固相法进行，并且发现合成肽在钙的存在下表现出乳糖结合活性。
In order to examine the correlation between the amino acid sequence and sugar binding specificity ofBauhinia purpurealectin (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.
双花豆种子凝集素的 cDNA 克隆和体外合成。
DOI：
10.1111/j.1432-1033.1987.tb13327.x
发表时间：
1987
期刊：
European journal of biochemistry
影响因子：
--
作者：
Schnell,DJ;Alexander,DC;Williams,BG;Etzler,ME
通讯作者：
Etzler,ME
来自红豆甙（Onobrychis viciifolia scop.）的凝集素。
影响因子：
2.9
作者：
Kouchalakos,RN;Bates,OJ;Bradshaw,RA;Hapner,KD
通讯作者：
Hapner,KD