Abstract
Summary
Streptokinase was prepared by ion-exchange chromatography on DEAE cellulose after prior treatment with (NH4)2SO4 or hydroxylapatite. The final product had 22-40% of the starting activity and 3-5% of the initial absorbance (280mμ). Streptokinase and streptococcal proteinase were found to be quite dissimilar proteins, and streptokinase was shown to be a substrate for trypsin which protected the latter against autolysis and DFP inhibition.
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