title: Characteristics of human milk glutathione peroxidase.
abstract: Human milk glutathione peroxidase (GPx) was purified 4500-fold using acetone precipitation and purification by repetitive ion-exchange and gel filtration chromatography with an overall yield of 34%. Homogeneity was established by gel electrophoresis. Using gel filtration, the molecular weight (mol wt) of the enzyme was estimated to be 92 kdalton (kD). The monomeric molecular weight was estimated to b 23 kD from polyacrylamide gel electrophoresis, indicating that the native enzyme consists of four identical subunits. The molecular weight of each subunit was supported by amino acid analysis. Selenium (Se) content of the purified enzyme was 0.31%, in a stoichiometry of 3.7 g-atoms/mol. Data from these studies reveal that GPx provided approximately 22% of total milk Se, but only 0.025% of the total protein.
authors.affiliation: Department of Food Science, University of Illinois, Urbana 61801.
authors.forename: I D
authors.initials: ID
authors.lastname: Bhattacharya
authors.forename: M F
authors.initials: MF
authors.lastname: Picciano
authors.forename: J A
authors.initials: JA
authors.lastname: Milner
mesh_terms: D000596:Amino Acids / Q000032:analysis; D005260:Female; D005979:Glutathione Peroxidase / Q000032:analysis*; D006801:Humans; D008895:Milk, Human / Q000201:enzymology*
chemical_list: D000596:Amino Acids; D005979:Glutathione Peroxidase