Complete amino acid sequence of Japanese chestnut agglutinin.
Complete amino acid sequence of Japanese chestnut agglutinin.
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日本板栗凝集素的完整氨基酸序列。
DOI：
10.1006/bbrc.2000.3420
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发表时间：
2000
影响因子：
3.1
通讯作者：
T. Nakanishi
中科院分区：
文献类型：
--
作者：
K. Nomura;S. Nakamura;M. Fujitake;T. Nakanishi
日本栗（Castanea crenata Sieb.）等Zucc。）凝集素（CCA）测定。通过胃蛋白酶消化获得的酸性肽的西姆斯分析显示N-末端氨基酸序列应为Acetyl-Met-Glu-Glu。在序列分析之前，半胱氨酸残基的重新测定表明每个亚基存在一个半胱氨酸残基。通过内切蛋白酶Arg-C和无色杆菌蛋白酶I消化以及溴化氰切割来确定完整序列。CCA由309个氨基酸残基组成，具有高含量的甘氨酸（16.5mol%）和一个半胱氨酸残基。计算的分子量为33，387 Da，包括N-末端乙酰基。完整的CCA的C-末端序列分析只得到一个序列，HMEYF，表明没有异质CCA形成的翻译后切割在C-末端区域，发生在一些豆类凝集素。对CCA自身序列的分析表明，CCA可分为两个结构域，N-结构域和C-结构域，几乎在中心。这些结构域共享约35%的相同残基，因此CCA具有重复序列。此外，这两个结构域显示出与jacalin相关凝集素的同源性，具有27-38%的同一性。这些结果表明，CCA的结构类似于两个分子的jacalin相关的凝集素。
The complete amino acid sequence of Japanese chestnut (Castanea crenata Sieb. et Zucc.) agglutinin (CCA) was determined. Analysis by SIMS of the acidic peptide obtained by pepsin digestion revealed that the N-terminal amino acid sequence should be Acetyl-Met-Glu-Glu. Prior to sequence analysis, redetermination of cysteine residues indicated the presence of one cysteine residue per subunit. The complete sequence was determined by endoproteinase Arg-C and Achromobacter protease I digestion, and CNBr cleavage. CCA consists of 309 amino acid residues with a high content of glycine (16.5 mol%) and one cysteine residue. The calculated molecular mass was 33, 387 Da including the N-terminal acetyl group. C-terminal sequence analysis of intact CCA gave only one sequence, HMEYF, indicating that no heterogeneous CCA formed by posttranslational cleavage at the C-terminal region, as occurs in some legume lectins. Analysis of the sequence of CCA itself revealed that CCA could be divided into two structural domains, the N-domain and the C-domain, almost at the center. These domains share about 35% identical residues, so CCA has a repeat sequence. Also, both domains show a homology to jacalin-related lectins with 27-38% identity. These results suggest that the structure of CCA resembles two molecules of jacalin-related lectin.