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Thromb Haemost 1994; 72(04): 595-603
DOI: 10.1055/s-0038-1648921
Original Article
Schattauer GmbH Stuttgart

Characterization of a Novel Streptokinase Produced by Streptococcus equisimilis of Non-Human Origin

Stephen T Nowicki
1   The Department of Medicine, College of Medicine, University of Florida, Gainesville, FL, USA
,
Dena Minning-Wenz
1   The Department of Medicine, College of Medicine, University of Florida, Gainesville, FL, USA
,
Kenneth H Johnston
2   The Department of Microbiology, Immunology and Parasitology, Louisiana State University Medical Center, New Orleans, LA, USA
,
Richard Lottenberg
1   The Department of Medicine, College of Medicine, University of Florida, Gainesville, FL, USA
› Author Affiliations
Further Information

Publication History

Received 01 March 1994

Accepted after revision 15 June 1994

Publication Date:
06 July 2018 (online)

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Summary

Streptokinases are proteins with plasminogen activator activity produced by certain hemolytic streptococci. We previously identified equine streptococcal isolates which produced streptokinases (ESKs) that bound both human and equine plasminogen but only readily activated equine plasminogen (14). This property was exploited to purify a representative ESK produced by Streptococcus equisimilis strain 87-542-W. Affinity chromatography with human plasminogen resulted in the isolation of a M~49,000 molecule with two isoforms. This ESK was subsequently compared to well characterized streptokinases (HSKs) that efficiently activate human plasminogen. Differences in streptokinases were identified in the highly conserved amino-terminal amino acid sequence, peptide maps, and antigenic properties, and these differences were supported by DNA hybridization studies. These results indicate that the family of proteins identified as streptokinases has much greater diversity than previously appreciated.

 

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