Adsorption of human serum albumin to microcrystalline cellulose interface h
as been determined as functions of protein concentration and pH of the aque
ous solutions. The maximum adsorption value is reached at the protein isoel
ectric point. The study of adsorption at several values of pH indicates tha
t its interaction with the MCC interface is not controlled by the electrost
atic effect. The FTIR, C-13 NMR data reveal that human serum albumin denatu
rates at its IEP and its macromolecules become extended. Resulting intercal
ates consist of microcrystalline cellulose, albumin, and solvent.