Disease relevance of MGC133817

• Calf thymus glutaredoxin is extended at both ends and has 31% overall residue identities with the corresponding E. coli protein [1].

High impact information on MGC133817

• Amino acid sequence comparison suggests that 11E belongs to the glutaredoxin family, but is unique so far in containing a signal sequence for endoplasmic reticulum membrane translocation [2].
• Glutaredoxin from calf thymus. Purification to homogeneity [3].
• Glutaredoxin, purified 3000-fold was demonstrated to be homogeneous by polyacrylamide gel electrophoresis and high performance liquid chromatography [3].
• As the concentration of the oxidant system was decreased stepwise from 1 mM to 1 microM to mimic conditions that may be associated with oxidative tissue injury in situ, deactivation of thioredoxin was decreased proportionately, whereas thioltransferase remained much more susceptible [4].
• Thioltransferase activity of bovine lens glutathione S-transferase [5].

Chemical compound and disease context of MGC133817

• The primary structure of calf thymus glutaredoxin. Homology with the corresponding Escherichia coli protein but elongation at both ends and with an additional half-cystine/cysteine pair [1].

Biological context of MGC133817

• This active center is identical in amino acid sequence and similar in position to that of Escherichia coli glutaredoxin, suggesting this structure to be typical for glutaredoxins and distinguishing them from the distantly related thioredoxins [1].
• The GSH/GSSG ratio and total dethiolase activity (thioltransferase and thioredoxin systems) remained unchanged relative to control hearts, indicating that overall redox status and sulfhydryl repair activity are maintained during moderate oxidative stress in situ [4].
• Immunochemical characterization and tissue distribution of glutaredoxin (thioltransferase) from calf [6].
• Particularly striking were observations of strong glutaredoxin immunoreactivity in oocytes in the ovary and the pattern of glutaredoxin in epithelial tissue of the skin and tongue reflecting differential expression during cell differentiation [6].
• A glutathione binding site at the dithiol region of glutaredoxin may be of primary importance for its function in protein dethiolation, while a different specific peptide binding site in thioredoxin may be more suited to certain protein disulfide structures [7].

Anatomical context of MGC133817

• A revised sequence of calf thymus glutaredoxin [8].
• Characterization of multiple acid phosphatases in bovine liver cytosol and lysosome. Inactivation of cytosolic enzymes by disulfides and its redox regulation by thioltransferase [9].
• Thioltransferase activity was found in cytosol of various bovine tissues [10].
• Inhibition of bovine leukocyte thioltransferase by anti-inflammatory drugs and anti-histaminic drugs [11].
• Isoelectric point (pI) of 8.3 for leukocyte thioltransferase was quite different from pI of 6.5 for erythrocyte enzyme [11].

Associations of MGC133817 with chemical compounds

• In contrast to the bacterial glutaredoxin, the calf thymus protein contains two additional half-cystines/cysteine residues at positions 74 and 78, which may be of regulatory significance [1].
• This method involved a pI-shift of glutaredoxin, obtained after oxidation of the fully reduced form with hydroxyethyl-disulfide, followed by CM-Sepharose chromatography [6].

Regulatory relationships of MGC133817

• There were some exceptions: e.g., follicular cells in the ovary did not contain immunohistochemically demonstrable glutaredoxin but expressed thioredoxin [6].

Analytical, diagnostic and therapeutic context of MGC133817

• Using these antibodies the distribution of glutaredoxin was mapped in calf organs and tissues by Western blots and by immunohistochemistry [6].
• Thioltransferase was purified 650-fold from rabbit liver by procedures including acid treatment, heat treatment, gel filtration on Sephadex G-50, column chromatography on DEAE-cellulose, isoelectric focusing (pH 3.5-10) and gel filtration on Sephadex G-75 [12].
• Thioltransferase was partially purified from bovine leukocyte using sonication, heat treatment at pH 5.1, Sephadex G-50 gel filtration and isoelectric focusing techniques [11].

References