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Thromb Haemost 1976; 35(02): 437-446
DOI: 10.1055/s-0038-1647938
Original Article
Schattauer GmbH

Studies on the Action Mechanism of the Antihemostatic Effect of lodopeptides[*]

A.L Golub
1   Department of Biochemistry, University of Miami, School of Medicine, P. O. Box 520875, Miami, Florida 33152
,
T.J Mende
1   Department of Biochemistry, University of Miami, School of Medicine, P. O. Box 520875, Miami, Florida 33152
› Author Affiliations
Further Information

Publication History

Received 23 March 1975

Accepted 10 October 1975

Publication Date:
02 July 2018 (online)

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Summary

A synthetic iodopeptide having a glutamic acid-diiodotyrosine molar ratio of 1:1 has been shown to be an effective anticoagulant both in vivo and in vitro. Contrasted with heparin the following general conclusions may be made regarding its action. The iodopeptide does not act through the inactivation of thrombin in plasma. Iodopeptide does interact with fibrinogen to form a complex which, in vitro, is not soluble in buffered saline at physiological pH. At pH 8, iodopeptide interacts with fibrinogen to form a soluble complex in the presence of 0.9 % NaCl that is not coaguable either by thrombin or Crotalus venom enzymes. All the available evidence indicates that the fibrinogen to fibrin conversion is not inhibited under these conditions, but that fibrin, once formed, is not able to polymerize due to interference by iodopeptide. Similar results were obtained with heparin in vitro with thrombin-fibrinogen mixtures in the absence of NaCl.

Studies with Russell’s viper venom in native PRP strongly suggest that the iodopeptide also interferes with processes in the early coagulation pathway associated with prothrombin activation.

* This paper is dedicated to Professor Karl H. Slotta, on the occasion of his 80th birthday.


 

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