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Fluorescence properties and conformation of human milk bile salt activated lipase



Fluorescence properties and conformation of human milk bile salt activated lipase



International Journal of Biological Macromolecules 9(5): 294-296



The fluorescence properties of human milk bile salt-activated lipase (BAL) in aqueous solution at various pH and in the presence of denaturing reagents and bile salts have been studied by measuring the accessibility of tryptophan side chains to the iodide ion. The fluorescence quenching studies of BAL demonstrated that the BAL conformation was pH sensitive. At pH 7.5, in the presence of denaturing reagents, all of the BAL tryptophan became accessible to iodide, suggesting the presence of random conformation in this medium. The decrease in tryptophan accessibility to iodide with various bile salt activators was found to correlate with the corresponding activity of BAL with long chain triacylglycerol substrate.

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Accession: 005471683

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