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Bioinformatics analysis of schwanniomyces occidentalis alpha amylase secretion signal sequences

机译:西方产氏链霉菌α淀粉酶分泌信号序列的生物信息学分析

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The amy gene from schwaniomyces occidentalis which encodes a secretory alpha amylase isolated by primers that designed from sequences derived from Gene bank. The isolated gene is then cloned into a p426gpd vector. After cloning, the recombinant vector was transformed into E.Coli DH5x strain and recombinant vector was sent for sequencing by T7, T3 and a mid primer. After sequencing, the sequence of the alpha amylase gene is then converted to amino acid sequence and the new hypothetical protein was analyzed by several signal peptide analysis programs. The cleavage sites and intracellular localization of the protein inside the cell is detected by this analysis. The results showed that schwanniomyces occidentalis alpha amylase has a 25 amino acid long secretory signal peptide that is responsible for initiation of transportation of the enzyme across endoplasmic reticulum, through the secretory pathway and finally secretion out of the cell. Our result would prove very important not only for production of these enzymes but also protein analysis and creating the recombinant organism that produce these enzymes.
机译:来自西方猪油菌的amy基因,其编码一种分泌性α淀粉酶,该α淀粉酶是通过从来源于基因库的序列设计的引物分离得到的。然后将分离的基因克隆到p426gpd载体中。克隆后,将重组载体转化到大肠杆菌DH5x菌株中,并通过T7,T3和中间引物对重组载体进行测序。测序后,将α淀粉酶基因的序列转换为氨基酸序列,并通过几种信号肽分析程序对新的假设蛋白进行分析。通过该分析检测细胞内蛋白质的切割位点和细胞内定位。结果表明,西方雪氏酵母α淀粉酶具有25个氨基酸长的分泌信号肽,其负责通过分泌途径开始酶穿过内质网的运输,并最终分泌到细胞外。我们的结果将证明不仅对于产生这些酶非常重要,而且对蛋白质分析和产生产生这些酶的重组生物非常重要。

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