Модификация функциональных групп стрептокиназы при йодировании

Abstract

Modification of tyrosine residues was detected in streptokinase molecule during iodination. A nonlinear type of the modification reaction allowed to suppose that tyrosine residues were heterogenous. As shown by gel chromatography the modified streptokinase did not develops stable complexes with human plasminogen even at low ratios of iodine/streplokinase, however the activating effects of the streptokinase were maintained. During iodination the secondary structure of streptokinase appears to be altera, the level of which depended on the molar ratio iodine/streptokinasc.