Title : Changes in structure and in interactions of heat-treated bovine beta-lactoglobulin.

Pub. Date : 2008

PMID : 18855755






4 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 In the presence of retinol, the alpha-helix content of the secondary structure of heat-treated beta-LG is increased and the major portion of its secondary structure is helical. Vitamin A beta-lactoglobulin Bos taurus
2 Fluorescence results show that heat-treated beta-LG at 95 degrees C can still bind retinol. Vitamin A beta-lactoglobulin Bos taurus
3 The refolding of the tertiary structure of beta-LG heat-denatured at 95 degrees C may recreate a retinol binding site. Vitamin A beta-lactoglobulin Bos taurus
4 Surprisingly, the affinity of the new site for retinol is higher than that of native beta-LG; however, the apparent molar ratio is lower than one. Vitamin A beta-lactoglobulin Bos taurus