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- W2479148046 abstract "Pure delipidated bovine serum albumin (BSA) adsorbs onto ethanol-cleaned glass at a (Langrauir-type) plateau value of ≃ 1.8 µg/cm2, at bulk BSA concentrations > 2.5 mg/ml. The shape of the adsorption isotherm, the irreversibility of the adsorption, the continuing diffusion of BSA along the plane of adsorption, and the ease and speed with which BSA could be electrophoretically transported along the plane of adsorption without detaching from the glass, agree best with adsorption of a monolayer of tightly packed, partly dehydrated BSA molecules with their longitudinal axes perpendicular to the glass plate. The most likely conformation of the adsorbed BSA molecules is a close vertical stacking with alternating polarities, allowing a certain degree of electrostatic attraction between protein molecules, and causing a loss of water of hydration. A monolayer of vertically stacked BSA molecules also conforms well to the dimensions of dehydrated BSA derived from hydrodynamic data, and offers a satisfactory explanation for the strong increase in the diffusion coefficient of BSA in the adsorbed state. The observed 50% increase in electrophoretic mobility of adsorbed BSA (as compared to dissolved BSA) also agrees well with the mobility of cylindrical molecules oriented perpendicularly to the electric field. The dimensions of large unhydrated BSA molecules that most reasonably fit these observations and the other known data are: 22 Å x 29 Å x 135 Å." @default.
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- W2479148046 date "1984-02-10" @default.
- W2479148046 modified "2023-09-29" @default.
- W2479148046 title "Steric Considerations in Protein Adsorption" @default.
- W2479148046 doi "https://doi.org/10.1021/bk-1984-0240.ch012" @default.
- W2479148046 hasPublicationYear "1984" @default.
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