Abstract
Summary
Chemical fractionation of a currently available, partially purified streptokinase-streptodornase concentrate yielded a 4-5 fold purification of the streptokinase. The addition of a starch zone electrophoresis to the methods increased the purification to 6-7 fold. Biophysical examination suggested that the protein was largely homogenous, but immunochemical analysis revealed the presence of extraneous antigenic components. Ultracentrifuge examination suggested that streptokinase has a molecular weight of approximately 50,000.
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