粘质沙雷氏菌
核酸酶
大肠杆菌
生物化学
肽序列
酶
DNA
蛋白质一级结构
生物
氨基酸
肠杆菌科
质粒
化学
基因
作者
Kirsten Biedermann,Pia Knak Jepsen,Erik Riise,Ib Svendsen
摘要
The primary structure and physical chemical properties were determined of a nuclease expressed and secreted by Escherichia coli. The plasmid p403-SD2 carried a DNA sequence isolated from Serratia marcescens encoding the enzyme. During cultivation of the E. coli cells, 85% of the enzyme was released to the growth medium. The enzyme was purified and exhibited a single band with a molecular weight about 30,600 daltons on SDS-PAGE similar to nuclease isolated from S. marcescens. The amino acid composition and the amino acid sequence determined directly confirmed the primary structure of 245 amino acids predicted from the DNA sequence, and, in addition, the two disulfide bridges were assigned. Several physical chemical properties were examined. The ability of the enzyme to cross the outer membrane is proposed to depend upon the formation of the proper structures during the folding process.
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