Rahman M A, Nelson H, Weissbach H, Brot N
Roche Institute of Molecular Biology, Roche Research Center, Nutley, New Jersey 07110.
J Biol Chem. 1992 Aug 5;267(22):15549-51.
The gene encoding peptide methionine sulfoxide reductase was cloned from an Escherichia coli genomic library using an oligonucleotide probe based on the amino-terminal sequence of the protein. The nucleotide sequence revealed that the gene codes for a polypeptide of 212 amino acid residues with a calculated molecular weight of 23,314. The protein has been overexpressed in E. coli and is present as a soluble active species.
利用基于该蛋白质氨基末端序列的寡核苷酸探针,从大肠杆菌基因组文库中克隆出编码肽甲硫氨酸亚砜还原酶的基因。核苷酸序列显示,该基因编码一个由212个氨基酸残基组成的多肽,计算分子量为23314。该蛋白质已在大肠杆菌中过表达,并以可溶性活性形式存在。