Purification of recombinant ribonuclease T1 expressed in Escherichia coli.
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.
Shirley
B A
BA
Department of Biochemistry and Biophysics, Texas A&M University, College Station 77843.
Laurents
D V
DV
D001230:Aspergillus / Q000201:enzymology*; D001236:Aspergillus oryzae / Q000201:enzymology*; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004722:Endoribonucleases / Q000302:isolation & purification*; D004926:Escherichia coli / Q000235:genetics; D011994:Recombinant Proteins / Q000302:isolation & purification; D006163:Ribonuclease T1 / Q000302:isolation & purification*
D011994:Recombinant Proteins; D004722:Endoribonucleases; D006163:Ribonuclease T1