Rat liver thioredoxin and thioredoxin reductase: purification and characterization.

  title={Rat liver thioredoxin and thioredoxin reductase: purification and characterization.},
  author={Marguerite Luthman and Anne Holmgren},
  volume={21 26},
A reproducible scheme has been developed for the preparation of rat liver thioredoxin and thioredoxin reductase (EC by using assays based on reduction of insulin and 5,5'-dithiobis(2-nitrobenzoic acid), respectively. Both proteins were purified to homogeneity, as judged from polyacrylamide gel electrophoresis. Thioredoxin had a molecular weight of 12 000 and contained about 110 amino acids including 4 half-cystines and an NH2-terminal valine. Peptide maps of reduced and… 

Human Placenta Thioredoxin Reductase

In its physiological, NADPH-reduced form, the enzyme is strongly inhibited by organic gold compounds that are widely used in the treatment of rheumatoid arthritis; for auranofin, the K i was 4 nm when measured in the presence of 50 μmthioredoxin.

Mitochondrial thioredoxin reductase in bovine adrenal cortex

The data clearly show that mitochondria, which might have originated from symbiotic prokaryotes, contain thioredoxin reductase similar to the cytosolic enzyme and different from the bacterial one.

An f-type thioredoxin fromArabidopsis thaliana Leaves

The purified f-type thioredoxin is the first example isolated from Arabidopsis thaliana and its molecular weight is not consistent with those of the five divergent h-typeThioredoxins already identified by cDNA cloning.

Thioredoxin-thioredoxin reductase--a system that has come of age.

    C. Williams
    Chemistry, Biology
    European journal of biochemistry
  • 2000
The thioredoxin–thiored toxin reductase system is verybroadly distributed and the two proteins have been isolated from many species and are similar to one another instructure and the conformation of the single domain is referred to as the thiOREDoxin fold with the redox-active disulfide form-ing a protrusion about 35 residues from the N-terminus.

Reduction of purothionin by the wheat seed thioredoxin system.

The results suggest that purothionin competes with ribonucleotide reductase for reducing equivalents from thioredoxin, and inhibition of deoxyribon nucleotide synthesis should be considered a possible mechanism when examining the toxic effects of purohionin on mammalian cells in S-phase.

Enzymatic reduction of alloxan by thioredoxin and NADPH-thioredoxin reductase.

    A. HolmgrenC. Lyckeborg
    Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1980
The toxic action of alloxan on animal cells, particularly the beta cells of pancreas, may be caused by rapid oxidation of cellular NADPH and generation of cytotoxic dialuric acid catalyzed by the thioredoxin system.

Thioredoxin reductase. Characterization of a homogenous preparation from Escherichia coli B.

    L. Thelander
    Biology, Chemistry
    The Journal of biological chemistry
  • 1967
Abstract Thioredoxin reductase (3) was purified by preparative polyacrylamide gel electrophoresis to give a preparation that appeared homogeneous by ultracentrifugal criteria, by chromatographic

Isolation and characterization of calf liver thioredoxin.

Thioredoxin reductase from rat liver.

    A. Larsson
    Biology, Chemistry
    European journal of biochemistry
  • 1973
A 100-fold-purification of thioredoxin reductase was obtained by treatment at pH 5 and chromatography on Sephadex and on DEAE-cellulose and this enzyme has now been purified from the same source.

Purification of Thioredoxin from Rat Novikoff Ascites Hepatoma

Although purification of thioredoxin reductase to electrophoretic homogeneity was not attained in these experiments, a molecular weight value of about 66,700 was estimated by gel filtration and 1-Dimethylaminonaphthalene-5-sulfonyl determination indicated valine to be the sole NH2-terminal amino acid.

Thioredoxin 2: cleavage with cyanogen bromide.

A simple and highly reproducible method for the preparation of thioredoxin from Escherichia coli B was worked out. On treatment with cyanogen bromide thioredoxin was cleaved into two peptides