Abstract
Three polysulphates [heparin, dextran sulphate (DS) and polyvinyl sulphate (PVS)] stimulated inactivation of trypsin in the absence of NaCl, but only PVS stimulated it in 0.1 m NaCl. The inactivation of trypsin depended on time and temperature and was not restored by adding NaCl. Stimulation by heparin of the trypsin inactivation was slightly protected by albumin. Long interaction of trypsin with DS was not essential to stimulate the enzyme inactivation. The intrinsic fluorescence of trypsin changed instantaneously by adding DS in the absence of NaCl, and it decreased more rapidly than the native enzyme. All these results indicate that trypsin molecules interacted once with the polysulphates are more labile and inactivated rapidly and irreversibly than the native molecules. Inactivation of plasmin was also stimulated by these polysulphates in the presence of 0.1 m NaCl, indicating that their interactions were stronger than the polysulphate-trypsin interaction.
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