[The conformation properties and conformation stability of streptokinase and its polymer derivative].
The properties and conformational stability of the proteinaceous activator of fibrinolysis--native streptokinase--and its derivative obtained by modification with a linear hydrophilic copolymer based on N-vinylpyrrolidone, were studied by the circular dichroism method. It was shown that polymeric modification of streptokinase had no effect on the secondary structure, while the conformational stability of the modified protein to urea was higher than that of the native one. Studies on thermal stability of both native and modified forms of streptokinase showed that the inactivation rate was lower in the modified form as compared to the native one.
D000595:Amino Acid Sequence; D002850:Chromatography, Gel; D002942:Circular Dichroism; D011205:Povidone / Q000031:analogs & derivatives* / Q000032:analysis; D011487:Protein Conformation; D011489:Protein Denaturation; D013300:Streptokinase / Q000032:analysis*
C047497:streptokinase-N-vinylpyrrolidone copolymer; D013300:Streptokinase; D011205:Povidone
Izuchenie konformatsionnykh svoĭstv i konformatsionnoĭ stabil'nosti streptokinazy i ee polimernogo proizvodnogo.