chondroitin-sulfates and succinyl-trialanine-4-nitroanilide

Chondroitin sulfates with different properties and devoid of appreciable anticoagulant activity were evaluated for their capacity to inhibit human leukocyte elastase activity in vitro by using a chromogenic substrate. Fractions with various mass and the same charge density were tested. The chondroitin sulfates with a molecular mass greater than about 2000 inhibited human leukocyte elastase activity to the same extent, whilst the fractions with a molecular mass of 1960 and 1020 were much less effective. The percentage inhibition of human leukocyte elastase activity increased based on the charge density of chondroitin sulfates. In particular, the inhibition of the enzymatic activity decreased with the percentage of non-sulfated disaccharide and increased with the amount of disaccharide-2,6-disulfated.

Topics: Animals; Anticoagulants; Chondroitin Lyases; Chondroitin Sulfates; Chromatography, Ion Exchange; Chromogenic Compounds; Disaccharides; Enzyme Inhibitors; Humans; Leukocyte Elastase; Molecular Structure; Molecular Weight; Oligopeptides; Sharks; Structure-Activity Relationship; Sulfates