Конформационные особенности молекул плазминогена человека, быка и кролика в растворе

Abstract

The differences in ionization of thyrosine residues, triptophan fluorescence, secondary and tertiary structures of the human, rabbit and bovine plasminogens were estimated. It is supposed that the ability of human plasminogen to form stable equimolar complexes with streptokinase can be ascribed to a smaller rigidity of its molecules in comparison with other plasminogens.