D. Muller

TL;DR: Diethylaminoethyl-dextrans with a relatively low percentage of dextran units bearing DEAE functions were layered on silica beads in order to determine the optimal conditions for the SEC of proteins.

TL;DR: Three sulphated polysaccharides were fractionated according to their affinity towards antithrombin III (ATIII) and heparin cofactor II (HCII), the two main physiological thrombin (IIa) inhibitors to study the possible presence of a unique binding site for ATIII and HCII.

TL;DR: The results obtained confirmed the importance of the arginyl residues grafted onto these polymers to obtain an affinity matrix useful for purifying thrombin with a high specific activity and a good recovery.

TL;DR: Insoluble polystyrenes substituted with sulphonate and L-arginyl methyl ester (PAOM) present substituents mimicking the reactive binding site of antithrombin III, which can be used as stationary phases in affinity liquid chromatography in order to purify thrombin with a high biological activity.

TL;DR: The pancreas contains two very analogous enzymes: trypsin and chymotrypsin, and amidine derivatives are synthesised and immobilised them with or without spacer arm on silica beads previously coated by dextran substituted with a calculated amount of positively charged diethylaminoethyl functions to minimize the non-specific interactions of silanol groups of the silica material.