Partial purification and properties of a plasminogen activator from human erythrocytes

M. Semar; L. Skoza; A. J. Johnson

doi: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: PubMed | Google Scholar

¹Department of Medicine, New York University Medical Center, and the American National Red Cross Research Laboratory, New York 10016

Find articles by Johnson, A. in: PubMed | Google Scholar

Published in Volume 48, Issue 10 on October 1, 1969
J Clin Invest. 1969;48(10):1777–1785. https://doi.org/10.1172/JCI106144.
© 1969 The American Society for Clinical Investigation

Published October 1, 1969 - Version history

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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