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   <subfield code="a">Purification and characterization of a novel fungi Se-containing protein from Se-enriched Ganoderma Lucidum mushroom and its Se-dependent radical scavenging activity</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[Ming Du, Lei Zhao, Chaorui Li, Guanghua Zhao, Xiaosong Hu]</subfield>
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   <subfield code="a">Our previous studies have established that Ganoderma lucidum (GL) can biotransform inorganic selenium into organic selenium, which was stored preferentially in its water-soluble protein component. In the present study, a novel water-soluble fungi Se-containing protein, named as Se-GL-P, has been purified for the first time from the Se-enriched GL to establish the relationship between the antioxidant activity of protein and its Se content. This protein was isolated and purified to homogeneity using ammonium sulfate precipitation followed by two consecutive anion exchange chromatography and size exclusion chromatography. This protein in its native state was identified as a monomer of 36,600Da estimated by 19.8% weight carbohydrate. The protein is acidic (pI=4.0) and rich in Asp, Glu, Gly, and Ala. The N-terminal shows a sequence of DINGGGATLPQKLYLTPDVL, suggesting that this protein belongs to a family of D I N G protein. The Se-content of this protein (4.87mg Se/g protein) is ∼3-fold larger than that of the water-soluble protein extract (1.91mg Se per protein). Perfectly consistent with its higher Se-content, the protein exhibits approximately three times stronger activity of scavenging superoxide and hydroxyl radicals as compared to the water-soluble protein extract, a finding demonstrating that the increasing antioxidant property of this protein depends quantitatively on its Se content.</subfield>
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