Preventive Nutrition and Food Science

The Korean Society of Food Science and Nutrition (한국식품영양과학회)
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Elctrophoretic Properties of Heat-Induced Bovine α-Lactalbumin

  • Lee, You-Ra (Department of Food and Nutrition, Chonnam National University) ;
  • Hong, Youn-Ho (Department of Food and Nutrition, Chonnam National University)
  • Published : 2002.03.01
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Abstract

In order to study the reaction behavior of bovine holo- and apo-$\alpha$-lactalbumin ($\alpha$-La) during heat treatment at 65~10$0^{\circ}C$, the samples were analysed by first (ID)-and second-dimensional (2D) native-polyacrylamide gel electrophoresis (Native-PAGE) and sodium dodecylsulfate (SDS)-PAGE. When bolo-$\alpha$-La or apo- $\alpha$ -La were heated, they formed non-native, monomers, dimers and trimers. The apo-$\alpha$-La was more heat-sensitive than holo-$\alpha$-La. The monomers seemed to have the same composition as the native $\alpha$-La, but many of the disulfide bonds could be non-native.

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