Previous work suggests albumin undergoes a conformational change in order to bind irreversibly to substrate. Using total internal reflectance fluorimetry (TIRF) and pulse laser excitation, we measured the fluorescence lifetimes of tryptophan and other residues of bovine serum albumin monomer (BSA) in order to examine this concept. These studies support the hypothesis that the adsorbed albumin exists in the form of a two-layer deposit, each with a possible different structure. The decrease in fluorescence lifetime of BSA when it adsorbs to quartz implies a corresponding change in quantum yield. Changes in the quantum yields of the fluorophoric residues of adsorbed BSA implies that the method of quantifying protein adsorption on surfaces by monitoring intrinsic fluorescence in TIRF cells is not reliable.
|Original language||English (US)|
|Title of host publication||Transactions of the Annual Meeting of the Society for Biomaterials in conjunction with the Interna|
|Place of Publication||San Antonio, TX, USA|
|Publisher||Soc for Biomaterials|
|Number of pages||1|
|State||Published - 1985|
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