他马汀
生物
互补DNA
克隆(编程)
大肠杆菌
品酒
分子克隆
遗传学
分子生物学
基因
葡萄酒
食品科学
计算机科学
程序设计语言
作者
Luppo Edens,L. Heslinga,Rob Klok,Ledeboer Am,Jaap Maat,Toonen My,Chris J. Visser,Verrips Ct
出处
期刊:Gene
[Elsevier]
日期:1982-04-01
卷期号:18 (1): 1-12
被引量:207
标识
DOI:10.1016/0378-1119(82)90050-6
摘要
The structural gene of the sweet-tasting plant protein (prepro) thaumatin was cloned and expressed in Escherichia colt. Expression was effected under control of lac and trp promoter/operator systems and through the use of bacterial ribosome-binding sites. The naturally occurring thaumatin II represents a processed form. The primary translation product, preprothaumatin, of the cloned mRNA-derived cDNA contains extensions at both the amino terminus and the carboxy terminus. The amino terminal extension of 22 amino acids is hydrophobic and very much resembles an excretion-related signal sequence. The six amino acids-long carboxy terminal extension is very acidic in character, in contrast to the overall highly basic thaumatin molecule. The possible role of such an acidic tail with respect to compartmentalization is discussed.
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