Gamma-Glycerylpropylsilyl or "glycophase" glass has been promoted as a non-fouling surface, resistant to protein adsorption and cell attachment, on which one can immobilize oligopeptide ligands, and thus create cell-type-specific culture surfaces. The present study confirmed that the glycerol-rich glycophase surface is a useful support for peptide immobilization. But glycophase glass was observed to adsorb more albumin than glass. At pH 7.4, desorption studies revealed that albumin bound more tightly to glycophase glass than to glass. Moreover, the growth rates, morphologies, and functions of transgenic betaG I/17 insulinoma cell cultures were equivalent on the two surfaces. Glycophase glass is neither protein- nor cell-repellant.