Some Properties of Flavoprotein in Quail Egg White

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  • ウズラ卵白フラボプロテインの分画とその特性
  • ウズラ ランパク フラボプロテイン ノ ブンカク ト ソノ トクセイ

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Abstract

The crude flavoproteins isolated from fresh quail and hen's egg white proteins by ammonium sulfate precipitation were further fractionated into two components (I and II peak) by DEAE-sephadex A-50 column chromatography. The flavoprotein content in quail was 1.5 fold higher than in hen's egg white. On SDS-PAGE, I and II peaks from quail migrated faster than those of flavoproteins from hen. Riboflavin binding capacity of apoproteins from quail and hen's egg white was 1:1 (riboflavin/protein molar ratio). The amino acid composition of flavoprotein was characterized by a high content of acidic amino acid, serine, cystein and a low content of threonine in both quail and hen, but no difference was found in the amino acid compositions of the flavoproteins from quail and hen. In the carbohydrate composition of the flavoprotein, galactose, glucosamine andsialic acid contents were higher in the hen's egg flavoprotein.

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