Abstract
Examination of conditions needed to form albumin microparticles (in the 1–5 μm diam. size range) by glutaraldehyde cross-linking, at low temperature (–15°C), suggested that the particles formed very rapidly over a short time scale and at low concentrations of cross-linking reagent. Detailed analysis showed that the particles increased in size with time of reaction and with an increase in glutaraldehyde concentration. Evaluation of the particle matrix using a dilute trypsin digestion process suggested that the above factors may influence the internal composition since the particles dissolved less rapidly than might be anticipated from a consideration of particle diameter alone.