大肠杆菌部分二倍体高水平生产β-半乳糖苷酶。
High-level production of -galactosidase by Escherichia coli merodiploids.
作者信息
Fowler A V
出版信息
J Bacteriol. 1972 Nov;112(2):856-60. doi: 10.1128/jb.112.2.856-860.1972.
Abstract
Two merodiploids of Escherichia coli that contain genes for the lac operon on both chromosome and episome were tested for production of lac enzymes after growth on various carbon sources. The specific activity of beta-galactosidase (and of thiogalactoside transacetylase) was about twice that from haploid cells when grown on glycerol. With succinate as carbon source, the specific activity increased by an additional factor of 3. Up to 25% of the soluble cell protein is beta-galactosidase in these strains, one of which is inducible and the other constitutive. The enzyme is purified easily in high yield by ammonium sulfate fractionation and electrophoresis.
摘要
对两株大肠杆菌部分二倍体进行了测试，这两株菌的染色体和附加体上均含有乳糖操纵子基因，测试内容为它们在不同碳源上生长后乳糖酶的产生情况。当在甘油上生长时，β-半乳糖苷酶（以及硫代半乳糖苷转乙酰基酶）的比活性约为单倍体细胞的两倍。以琥珀酸盐作为碳源时，比活性又增加了3倍。在这些菌株中，可溶性细胞蛋白中高达25%是β-半乳糖苷酶，其中一株是可诱导型的，另一株是组成型的。通过硫酸铵分级分离和电泳，该酶很容易以高产率纯化。
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