Purification and characterization of an estrogen-binding peroxidase from human fetuses.
Biochimie, 1979;61(4):535-41.
Dimitrijevic L, Aussel C, Mucchielli A, Masseyeff R
PMID: 114237
Impact factor: 4.372
Abstract
A peroxidase found under two forms with a molecular weight of 220,000 and 170,000 respectively, was purified from human fetuses. The purification procedure included ammonium sulfate precipitation, ion exchange chromatography, gel filtration and hydrophobic interaction chromatography. The purification factor approximated 400. These two forms of peroxidase were found to be immunologically identical as shown when utilizing immunodiffusion. They were able to bind estradiol in the presence of H2O2. This bond resisted to denaturation and solvent extraction therefore suggesting a covalent binding of estradiol to the enzyme.
MeSH terms
Carrier Proteins; Chromatography, Gel; Chromatography, Ion Exchange; Estrogens; Fetus; Humans; Immunodiffusion; Molecular Weight; Peroxidases; Spectrometry, Fluorescence
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