Thromb Haemost 1979; 42(03): 924-928
DOI: 10.1055/s-0038-1666941
Original Article
Schattauer GmbH Stuttgart

Purification of Urokinase by a Beta-Naphthamidine Affinity Column

B Åstedt
The Research Laboratories of the Departments of Gynecology & Obstetrics and Pediatrics, University of Lund, Malmö Allmänna Sjukhus, 21401 Malmö, Sweden, the Section of Biosciences, Karl-Marx-University of Leipzig, GDR, and the Research Laboratories of Lowens Pharmaceuticals, Denmark
,
L Holmberg
The Research Laboratories of the Departments of Gynecology & Obstetrics and Pediatrics, University of Lund, Malmö Allmänna Sjukhus, 21401 Malmö, Sweden, the Section of Biosciences, Karl-Marx-University of Leipzig, GDR, and the Research Laboratories of Lowens Pharmaceuticals, Denmark
,
G Wagner
The Research Laboratories of the Departments of Gynecology & Obstetrics and Pediatrics, University of Lund, Malmö Allmänna Sjukhus, 21401 Malmö, Sweden, the Section of Biosciences, Karl-Marx-University of Leipzig, GDR, and the Research Laboratories of Lowens Pharmaceuticals, Denmark
,
P Richter
The Research Laboratories of the Departments of Gynecology & Obstetrics and Pediatrics, University of Lund, Malmö Allmänna Sjukhus, 21401 Malmö, Sweden, the Section of Biosciences, Karl-Marx-University of Leipzig, GDR, and the Research Laboratories of Lowens Pharmaceuticals, Denmark
,
J Ploug
The Research Laboratories of the Departments of Gynecology & Obstetrics and Pediatrics, University of Lund, Malmö Allmänna Sjukhus, 21401 Malmö, Sweden, the Section of Biosciences, Karl-Marx-University of Leipzig, GDR, and the Research Laboratories of Lowens Pharmaceuticals, Denmark
› Author Affiliations
Further Information

Publication History

Received 12 September 1978

Accepted 21 November 1978

Publication Date:
23 August 2018 (online)

Summary

Urokinase was purified by affinity chromatography using 6-amino-naphthamidine-(2), a new specific ligand based on the urokinase inhibitor β-naphthamidine. Urokinase was firmly bound at pH 7.0 and could be eluted at pH 3.0. The protein which passed the column at pH 7.0 without being bound did not contain any urokinase activity. This is an important property because it can be utilized for raising a monospecific urokinase antiserum by absorbing unspecific antibodies with only a minor loss of antiserum titre.

 
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