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首页> 外文期刊>Journal of Agricultural and Food Chemistry >Complete Amino Acid Sequence of the Lentil Trypsin-Chymotrypsin Inhibitor LCI-1.7 and a Discussion of Atypical Binding Sites of Bowman-Birk Inhibitors
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Complete Amino Acid Sequence of the Lentil Trypsin-Chymotrypsin Inhibitor LCI-1.7 and a Discussion of Atypical Binding Sites of Bowman-Birk Inhibitors

机译:小扁豆胰蛋白酶胰蛋白酶抑制剂LCI-1.7的完整氨基酸序列和Bowman-Birk抑制剂非典型结合位点的讨论

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摘要

The complete primary structure of the lentil (Lens culinaris) trypsin-chymotrypsin inhibitor LCI-1.7 was determined by conventional methods in order to find relationships between partial sequences and the difference in action against human and bovine chymotrypsin.As other Bowman-Birk type inhibitors,LCI-1.7 contained 68 amino acid residues,seven disulfide bridges,and two reactive sites,Arg16-Ser17 for trypsin and Tyr42-Ser43 for chymotrypsin.Evaluation of sequence homologies showed that it belonged to the group III Bowman-Birk inhibitors.The atypical additional binding site of LCI-1.7 for human chymotrypsin was discussed and compared with such binding sites of two other Bowman-Birk inhibitors,the Bowman-Birk soybean proteinase inhibitor BBI,and the lima bean proteinase inhibitor LBI I,for human and bovine trypsin and chymotrypsin.A concept to reduce the action of these inhibitors against human enzymes by genetic engineering was proposed.
机译:通过常规方法确定了小扁豆(Lens culinaris)胰蛋白酶-胰凝乳蛋白酶抑制剂LCI-1.7的完整一级结构,以发现部分序列与针对人和牛胰凝乳蛋白酶的作用差异之间的关系。作为其他Bowman-Birk型抑制剂, LCI-1.7包含68个氨基酸残基,七个二硫键和两个反应性位点,胰蛋白酶的Arg16-Ser17和胰凝乳蛋白酶的Tyr42-Ser43。序列同源性的评估表明它属于III类Bowman-Birk抑制剂。讨论了LCI-1.7与人胰凝乳蛋白酶的结合位点,并与另外两种Bowman-Birk抑制剂(Bowman-Birk大豆蛋白酶抑制剂BBI和利马豆蛋白酶抑制剂LBI I)的结合位点进行了比较,用于人和牛胰蛋白酶和糜蛋白酶提出了通过基因工程来减少这些抑制剂对人类酶的作用的概念。

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