polymer films were washed with cold de-ionized water to remove any residue from the reactions. The films were dried to a constant weight in a vacuum oven at 50 C at 0.1 mm Hg. Degradation was assessed by visual inspection of the polymers following filtration and drying. Each of the resulting aqueous filtrates was rotary evaporated at 60 C at 0.10 mm Hg. The residue was dissolved in CDC13 with TMS as an internal standard and examined by 1HNMR (300 MHz). Enzymatic Degradation of Glycinol Polymer (13) A 4.9 mg film was placed in buffered aqueous solution (1.0 mL, 0.02 M). A 4.0 mg film was placed in the pH 11.0 aqueous solution (1.0 mL). A 4.2 mg film was placed in a solution containing 70,000 units of the lipase from Rhizopus Arrhizus (dissolved in 0.2 mL of deionized water), 0.6 mL de-ionized water and 0.2 mL (0.1 M) phosphate buffer. A 4.9 mg film was placed in a solution containing 11,000 units of ca- chymotrypsin (dissolved in 0.2 mL of de-ionized water), 0.6 mL de-ionized water and 0.2 mL (0.1 M) phosphate buffer. A 4.6 mg film was placed in a solution containing 235,000 units of Trypsin (dissolved in 0.2 mL de-ionized water), 0.6 mL de-ionized water and 0.2 mL (0.1 M) phosphate buffer. A 5.3 mg film was placed in a solution containing 500 units of papain (dissolved in 0.2 mL de-ionized water), 0.6 mL de-ionized water and 0.2 mL (0.1 M) phosphate buffer. The solutions were shaken and incubated for approximately 100 hours. The resulting solutions were filtered on a Kontes apparatus using a 0.45 micron Teflon filter. The resultant film and residue were dried in a vacuum oven at 50 C until a constant weight was reached. Each film was visually inspected for evidence of degradation. The 1HNMR of the rotary evaporated filtrates revealed no degradation by products only phosphate buffer.