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Expression, Isolation, and Purification of Soluble and Insoluble Biotinylated Proteins for Nerve Tissue Regeneration
Published on: January 22, 2014
Purification of recombinant ribonuclease T1 expressed in Escherichia coli
1Department of Biochemistry and Biophysics, Texas A&M University, College Station 77843.
Journal of Biochemical and Biophysical Methods
|March 1, 1990
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.
