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Cited by 238

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The Purification and Properties of Glutathione Peroxidase of Erythrocytes

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Mills, Gordon C.·1959·Journal of Biological Chemistry

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).

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Metadata

Authors
Mills, G. C.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1959-03
Volume
234
Issue
3
Pages
502-506
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2098651583
Cited by
238
References
0
FWCI
2.57
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: The Purification and Properties of Glutathione Peroxidase of Erythrocytes. https://app.cochat.ai/papers/10.1016/s0021-9258(18)70234-2
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Mills, G. C. (1959). The Purification and Properties of Glutathione Peroxidase of Erythrocytes. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)70234-2

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