Use of mono Q high resolution ion exchange chromatography to obtain highly pure and active Escherichia coli RNA polymerase

Biochemistry ◽  
1990 ◽  
Vol 29 (34) ◽  
pp. 7890-7894 ◽  
Author(s):  
Dayle A. Hager ◽  
Ding Jun Jin ◽  
Richard R. Burgess
Keyword(s):  
Escherichia Coli ◽  
High Resolution ◽  
Ion Exchange ◽  
Rna Polymerase ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography

scholarly journals Heat-stable enterotoxins from Escherichia coli P16

1980 ◽  
Vol 28 (3) ◽  
pp. 1038-1040
Author(s):  
M N Burgess ◽  
N A Mullan ◽  
P M Newsome
Keyword(s):  
Escherichia Coli ◽  
Ion Exchange ◽  
Isoelectric Focusing ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Infant Mouse ◽  
Heat Stable

Escherichia coli P16 infant mouse active heat-stable enterotoxin may be fractionated into two distinct active moieties by ion-exchange chromatography, Sephadex G-25 chromatography, and isoelectric focusing.

scholarly journals Thiol-protein disulphide oxidoreductases. Differences between protein disulphide-isomerase and glutathione-insulin transhydrogenase activities in ox liver

1976 ◽  
Vol 159 (2) ◽  
pp. 385-393 ◽  
Author(s):  
H C Hawkins ◽  
R B Freedman
Keyword(s):  
High Resolution ◽  
Ion Exchange ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Heat Denaturation ◽  
Differential Centrifugation ◽  
Protein Disulphide Isomerase ◽  
Final Sample ◽  
Thiol Protein ◽  
Single Enzyme

1. Protein disulphide-isomerase and glutathione-insulin transhydrogenase activities were assayed in parallel through a conventional purification of protein disulphide-isomerase from ox liver. 2. Throughout a series of purification steps (differential centrifugation, acetone extraction, (NH4)2SO4 precipitation and ion-exchange chromatography), the two activities appeared in the same fractions but were purified to different extents. 3. The final sample was 143-fold purified in protein disulphide-isomerase but only 10-fold purified in glutathione-insulin transhydrogenase; nevertheless the two activities in this preparation were not resolved by high-resolution isoelectric focusing and both showed pI4.65. 4. In a partially purified preparation containing both activities, glutathione-insulin transhydrogenase was far more sensitive to heat denaturation than was protein disulphide-isomerase; conversely protein disulphide-isomerase was more sensitive to inactivation by deoxycholate. 5. The data are inconsistent with a single enzyme being responsible for all the protein disulphide-isomerase and glutathione-insulin transhydrogenase activity of ox liver. It is suggested that several similiar thiol-protein disulphide oxidoreductases of overlapping specificities may better account for the data.

High-resolution determination of 147Pm in urine using dynamic ion-exchange chromatography

1992 ◽  
Vol 64 (20) ◽  
pp. 2339-2343 ◽  
Author(s):  
Steve. Elchuk ◽  
Charles A. Lucy ◽  
Kerry I. Burns
Keyword(s):  
High Resolution ◽  
Ion Exchange ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography
Sign in / Sign up

Export Citation Format

Share Document