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Research Article Free access | 10.1172/JCI106144
1Department of Medicine, New York University Medical Center, and the American National Red Cross Research Laboratory, New York 10016
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1Department of Medicine, New York University Medical Center, and the American National Red Cross Research Laboratory, New York 10016
Find articles by Skoza, L. in: JCI | PubMed | Google Scholar
1Department of Medicine, New York University Medical Center, and the American National Red Cross Research Laboratory, New York 10016
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Published October 1, 1969 - More info
The lysis time of euglobulin clots made with whole blood (plasma and red cells) was very much shorter than that of clots made with plasma alone, indicating a fibrinolytic component in red cells. A plasminogen activator was found in the stroma-free hemolysate, and proteolytic activity was found in the stromal fraction. The plasminogen activator, purified by using diethylaminoethyl-cellulose (DEAE-cellulose) in a batch procedure followed by column chromatography, was called erythrokinase (EK). On preliminary characterization, EK appears to activate human and bovine plasminogen in a manner similar to urokinase (UK), as determined by fibrinolytic and caseinolytic assays. The two enzymes can be separated by DEAE chromatography and acrylamide-gel electrophoresis, however, and they hydrolyze acetyl-L-lysine methyl ester and benzoyl arginine methyl ester at different rates.
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