Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Purification and properties of a recombinant sulfur analog of murine selenium-glutathione peroxidase.

European journal of biochemistry - 1 May 1992

Rocher C, Lalanne J L, Chaudière J

Abstract excerpt

We previously constructed plasmids for synthesis of glutathione-peroxidase (GPx) mutants in an Escherichia coli expression system. In these recombinant proteins either cysteine ([Cys]GPx mutant) or serine ([Ser]GPx mutant) were present in place of the active-site selenocysteine (SeCys) of the natural enzyme. We have now investigated GPx activity of [Cys]GPx and [Ser]GPx mutants. Enzyme assays performed on...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cysteine
Share to Electrophoresis, Polyacrylamide Gel
Share to Escherichia coli

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Genes, Bacterial

Share to Hydrogen-Ion Concentration

Share to Mutation

Share to Recombinant Proteins

Source

Identifiers

PMID: 1577013
DOI: 10.1111/j.1432-1033.1992.tb16862.x

Genes

SDS

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Purification and properties of a recombinant sulfur analog of murine selenium-glutathione peroxidase.PMID 1577013Read ↗

Characterization and structural analysis of human selenium-dependent glutathione peroxidase 4 mutant expressed in Escherichia coli.Semantic proximity Read ↗

Cysteine mutant of mammalian GPx4 rescues cell death induced by disruption of the wild-type selenoenzyme.Semantic proximity Read ↗

Can recombinant human glutathione peroxidase 1 with high activity be efficiently produced in Escherichia coli ?Semantic proximity Read ↗

Unglycosylated recombinant human glutathione peroxidase 3 mutant from Escherichia coli is active as a monomer.Semantic proximity Read ↗

Different catalytic mechanisms in mammalian selenocysteine- and cysteine-containing methionine-R-sulfoxide reductases.Semantic proximity Read ↗

Overexpression of wild type and SeCys/Cys mutant of human thioredoxin reductase in E. coli: the role of selenocysteine in the catalytic activity.Semantic proximity Read ↗

Knockout of SOD1 promotes conversion of selenocysteine to dehydroalanine in murine hepatic GPX1 protein.Semantic proximity Read ↗

Biochemical characterizations of ER-resident peroxidases, GPx7 and GPx8, reveal their distinct and regulated oxidative activitiesSemantic proximity Read ↗

Studies of an active site mutant of the selenoprotein thioredoxin reductase: the Ser-Cys-Cys-Ser motif of the insect orthologue is not sufficient to replace the Cys-Sec dyad in the mammalian enzyme.Semantic proximity Read ↗

Improving Catalytic Activity, Acid-Tolerance, and Thermal Stability of Glutathione Peroxidase by Systematic Site-Directed Selenocysteine Incorporation.Semantic proximity Read ↗

Protein disulfide isomerase and glutathione are alternative substrates in the one Cys catalytic cycle of glutathione peroxidase 7.Semantic proximity Read ↗

Characterization of mitochondrial thioredoxin reductase from C. elegans.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.