Characteristics of human milk glutathione peroxidase |
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Authors: | Ira D Bhattacharya M F Picciano John A Milner |
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Institution: | 1. Department of Food Science, University of Illinois, 61801, Urbana, Illinois 2. Division of Nutritional Sciences, University of Illinois, 61801, Urbana, Illinois 3. School of Human Resources and Family Studies, University of Illinois, 61801, Urbana, Illinois
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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. |
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Keywords: | Index Entries" target="_blank">Index Entries Human milk glutathione peroxidase protein purification selenium |
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