Carbohydrate-Containing Derivatives of the Trypsin-Kallikrein Inhibitor Aprotinin from Bovine Organs. II. Inhibitor Coupled to the (Carboxymethyl)dextran Derivatives of D-Galactose

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Abstract
The trypsin-kallikrein inhibitor aprotinin was coupled to (carboxymethyl)dextran derivatives of D-galactose. The conjugates contained 14 and 38 D-galactose residues/mol of protein, respectively. The apparent dissociation constants (Ki) of the complexes between trypsin and modified aprotonins proved to be 1 order of magnitude higher than the respective values for native aprotinin. The distribution of the modified aprotinins in rat organs after endocardial injection was studied. The conjugates of aprotinin with (carboxymethyl)dextran derivatives of D-galactose were characterized by decreased clearance rates; they accumulated in the active form in liver. The accumulation was 2.5-10 times higher than native aprotinin for the time of observation (5 min to 2 h). [Aprotinin has been used in the treatment of some diseases caused by proteinases, such as pancreatitis and septicemia.].

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