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Abstract
Anticoagulation with heparin is required during extracorporeal circulation for hemodialysis
and cardiopulmonary bypass as well as during vascular surgery. Reversal of anticoagulation
with protamine may be associated with hypotension and rebound anticoagulation and
requires stoichiometric doses. Heparinase from Flavobacterium heparinum catalytically degrades heparin and reverses its anticoagulant effect. Heparin was
administered to New Zealand White rabbits and plasma levels were assayed with the
APTT anticoagulant assay and the azure A chemical assay. Heparinase actively degraded
heparin both in vitro in rabbit plasma and in vivo in rabbit blood as determined by
both the anticoagulant and chemical assays when compared to control heparin disappearance
curves. Antibodies to heparinase were demonstrated by the ELISA technique in rabbits
receiving i.v. heparinase. These antibodies, however, did not effect the activity
of the enzyme in vitro or in vivo. No toxic effects of heparinase were noted in observations
of the animals or in blood and histologic studies. Heparinase, either free or immobilized,
may be a useful heparin-reversing agent without the drawbacks of protamine.
Abbreviations:
(i.m.) (intramuscular(ly)), (i.v.) (intravenous(ly)), (APTT) (activated partial thromboplastin time), (ELISA) (enzyme-linked immunosorbent assay), (PBS) (phosphate-buffered saline), (SDS) (sodium dodecyl sulfate), (LDH) (lactic acid dehydrogenase), (SGOT) (serum glutamic oxaloacetic transaminase), (SGPT) (serum glutamic pyruvic transaminase)To read this article in full you will need to make a payment
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Article info
Publication history
Accepted:
July 26,
1983
Received:
January 18,
1983
Footnotes
☆Supported in part by NIH Grant GM25810.
Identification
Copyright
© 1983 Published by Elsevier Inc.
