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DOI: 10.1055/s-0038-1661022
Dysfunctional Plasminogen in Full Term Newborn - Study of Active Site of Plasmin
Publication History
Received 14 November 1983
Accepted 18 November 1983
Publication Date:
19 July 2018 (online)
![](https://www.thieme-connect.de/media/10.1055-s-00035024/198401/lookinside/thumbnails/10-1055-s-0038-1661022-1.jpg)
Summary
The functional activity and active site of plasmin in full-term newborns have been studied and compared to those in adults in order to investigate the nature of the abnormality found in newborn plasminogen descried in a previous paper.
The functional activity of newborn plasminogen measured on chromogenic substrate was approximately 18% that of adult plasminogen when streptokinase was used as an activator and 12% when urokinase was used.
Proteolysis of newborn plasminogen by urokinase yielding a two-chain plasmin form occurred normally, but the incorporation of diisopropylphosphorofluoridate into the light chain of newborn plasmin was approximately 23% of that observed in the light chain of adult plasmin.
These observations suggest that the abnormality of full-term newborn plasminogen is located in the active site of the molecule.
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