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Thromb Haemost 1978; 39(01): 046-052
DOI: 10.1055/s-0038-1646653
Original Article
Schattauer GmbH Stuttgart

The Effects of Metal Ions on Esterase Activities of Urokinase

Hiroyuki Sumi
The 2nd Department of Physiology, Hamamatsu University, School of Medicine, Hamamatsu, Shizuoka, Japan
,
Yumiko Takada
The 2nd Department of Physiology, Hamamatsu University, School of Medicine, Hamamatsu, Shizuoka, Japan
,
Akikazu Takada
The 2nd Department of Physiology, Hamamatsu University, School of Medicine, Hamamatsu, Shizuoka, Japan
› Author Affiliations
Further Information

Publication History

Received 06 March 1997

Accepted 20 June 1997

Publication Date:
12 July 2018 (online)

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Summary

The esterase activity of highly purified human urokinase on Nα-acetylglycyl-L-lysine methyl ester is strongly inhibited by 1 × 10-5tol × 10“2MCu++, Hg++, Ni++, Co++, Fe+++, and Mn++ solutions, whereas Na+, K+, Ca++, and Mg++ are weakly effective. This inhibition is parallel with the inhibition of activation of plasminogen by urokinase. There is no simple linear relation between inhibition and ion concentration. Addition of ethylenediaminetetraacetate or electrodialysis fully reactivates the inhibited enzyme. These results are discussed in relation to similar effects of ions on trypsin.

 

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