Abstract
The generation of active two chain urokinase from the proenzyme pro-urokinase by catalytic amounts of plasmin is an important regulatory step in plasminogen activation. The plasminogen activator, urokinase, converts plasminogen to plasmin which in turn dissolves fibrin blood clots. We have studied the conversion of pro-urokinase (Pro-UK) to high molecular weight urokinase (HMW-UK) by plasmin. This paper describes a peptide map that separates various plasmin cleavage products of Pro-UK/HMW-UK. A partially purified sample of HMW-UK containing trace amounts of plasmin was incubated at room temperature for 12 days. The digested peptide mixture after reduction and S-carbamide methylation was separated using reversed phase high performance liquid chromatography. The peptides were collected and analyzed for their N-terminal amino acid sequences, and in some cases by plasma desorption mass spectrometry (PDMS). The plasmin map so generated is useful in investigating the integrity of any HMW-UK produced via plasmin cleavage step.
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