The DOI matches its Crossref record; 18 of the 18 references it cites were found in a registry or an index.
Properties and Regulation of Glutathione Peroxidase
Open accessAbstract
Abstract GSH peroxidase has been purified approximately 2500-fold from pig's blood. With cumene hydroperoxide as substrate, kinetic analysis on the purified enzyme gave nonlinear Lineweaver-Burk plots for the hydroperoxide substrate. Linear Lineweaver-Burk plots were obtained for GSH and a limiting Km value of approximately 3 mm was obtained for GSH. A limited analysis of the rate data has been carried out and a tentative mechanism for GSH peroxidase is given. A wide range of nucleotides inhibited the enzyme, with pyrimidine nucleotides being the most effective. Also, the inhibitory effectiveness increased with the number of phosphate groups in the nucleotide. Nucleotide inhibition was competitive with respect to GSH whereas increased levels of hydroperoxide enhanced the inhibition. The sensitivity of the enzyme to nucleotide inhibition could be substantially decreased by x-ray, ethanol, or trypsin treatment, or aging with a lesser decrease of catalytic activity. Conversely, heat, p-chloromercuribenzoate, or sodium lauryl sulfate preferentially abolished the catalytic function with a lesser effect on the nucleotide response. It was concluded that nucleotides interact with the enzyme at a site other than the active center and hence that GSH peroxidase is an allosteric enzyme.
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Cites
PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Lowry, O., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 317,331
The Determination of Enzyme Dissociation Constants
Lineweaver, H., & Burk, D. (1934) · Journal of the American Chemical Society · doi:10.1021/ja01318a036 · Cited by 12,060
Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase.
Paglia, D. E., & Valentine, W. N. (1967) · PubMed · Cited by 10,889
Spectrophotometric Study of the Reaction of Protein Sulfhydryl Groups with Organic Mercurials
Boyer, P. D. (1954) · Journal of the American Chemical Society · doi:10.1021/ja01646a025 · Cited by 1,667
Space-Time Relationships in Somesthetic Localization
Jones, F. N. (1956) · Science · doi:10.1126/science.124.3220.484-a · Cited by 836
The Combinations of Haemoglobin with Oxygen and with Carbon Monoxide. I
Hill, A. V. (1913) · Biochemical Journal · doi:10.1042/bj0070471 · Cited by 800
Glutathione Peroxidase: The Primary Agent for the Elimination of Hydrogen Peroxide in Erythrocytes*
Cohen, G., & Hochstein, P. (1963) · Biochemistry · doi:10.1021/bi00906a038 · Cited by 666
Carbonic anhydrase. Purification and nature of the enzyme
Keilin, D., & Mann, T. (1940) · Biochemical Journal · doi:10.1042/bj0341163 · Cited by 493
An intracellular GSH-peroxidase with a lipid peroxide substrate
Little, C., & O'Brien, P. J. (1968) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(68)90721-3 · Cited by 445
Self-citationPinto, R. E., & Bartley, W. (1969) · Biochemical Journal · doi:10.1042/bj1120109 · Cited by 379
Cited by
Hydrogen Peroxide is Scavenged by Ascorbate-specific Peroxidase in Spinach Chloroplasts
Nakano, Y., & Asada, K. (1981) · Plant and Cell Physiology · doi:10.1093/oxfordjournals.pcp.a076232 · Cited by 10,809
Purification and properties of rat lung soluble glutathione peroxidase
Chiu, D. T. Y., Stults, F. H., & Tappel, A. L. (1976) · Biochimica et Biophysica Acta (BBA) - Enzymology · doi:10.1016/0005-2744(76)90110-8 · Cited by 349
van Hameren, G., Campbell, G., Deck, M., Berthelot, J., Gautier, B., Quintana, P., Chrast, R., & Tricaud, N. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0740-4 · Cited by 83
Attenuation of doxorubicin-induced cardiac injury by mitochondrial glutaredoxin 2
Diotte, N. M., Xiong, Y., Gao, J., Chua, B. H. L., & Ho, Y.-S. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.10.014 · Cited by 78
Metadata
- Authors
- Little, C., Olinescu, R., Reid, K. G., & O'Brien, P. J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1970-07
- Volume
- 245
- Issue
- 14
- Pages
- 3632-3636
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1495200985
- Cited by
- 259
- References
- 18
- FWCI
- 2.07
- Type
- journal article
- Language
- en
- Open access
- hybrid
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
