The Purification and Properties of Glutathione Peroxidase of Erythrocytes
Year: 1959
Type: article
Abstract: phenylhydrazine and hydrogen peroxide were prepared fresh as needed for the various experimental procedures. The hydrogen peroxide concentration was determined by titration with a standardized permanganate solution. Horseradish peroxidase was obtained from Nutritional Biochemicals Corporation. Diethylaminoethyl cellulose1 was prepared from Solka-Floe as described by Peterson and Sober (8). Titration curves of the lyophilized preparation showed the presence of 0.9 m.eq. of ionizing groups per gm. of dry material. Methods-All spectrophotometric measurements were made with a model DU Beckman spectrophotometer. Optical density readings at 270 rnp were used as a routine measure of the protein concentration in eluent fractions. The optical density readings at 270 rnp of a solution of the purified enzyme preparation were correlated with the protein nitrogen content of this same sample by a nitrogen analysis carried out by the Kjeldahl procedure (9). Catalase activity was measured by the method of Feinstein (10).
Source: Journal of Biological Chemistry
Author: Gordon C. Mills
Institution: The University of Texas Medical Branch at Galveston
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W2098651583