Purification of recombinant ribonuclease T1 expressed in Escherichia coli.
作者信息
Shirley B A, Laurents D V
机构信息
Department of Biochemistry and Biophysics, Texas A&M University, College Station 77843.
出版信息
J Biochem Biophys Methods. 1990 Mar;20(3):181-8. doi: 10.1016/0165-022x(90)90076-o.
PMID:2111835
Abstract
A protocol for the rapid purification of ribonuclease T1 expressed from a chemically synthesized gene cloned into Escherichia coli is described. QAE ion-exchange and Sephadex G-50 chromatography are used to give over 300 mg (88% yield) of pure ribonuclease T1 from 61 of liquid culture in 3 days. We also report a new absorption coefficient for RNase T1: E1%278 nm = 15.4.
摘要
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