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Thromb Haemost 1984; 52(01): 001-003
DOI: 10.1055/s-0038-1661122
Original Article
Schattauer GmbH Stuttgart

Clotting Enzyme Activity Derived from the Coelomocytes of the Sea Star, Asterias Forbesi

J A Marcum
1   The Department of Medicine, Harvard Medical School, Boston, MA, and Department of Biology, MIT, Cambridge, MA
4   The Marine Biological Laboratory, Woods Hole, MA, U.S.A.
,
J Levin
2   The Departments of Laboratory Medicine and Medicine, University of California School of Medicine, San Francisco, CA
4   The Marine Biological Laboratory, Woods Hole, MA, U.S.A.
,
R A Prendergast
3   The Department of Ophthalmology, The Johns Hopkins University School of Medicine, Baltimore, U.S.A.
4   The Marine Biological Laboratory, Woods Hole, MA, U.S.A.
› Author Affiliations
Further Information

Publication History

Received 13 April 1984

Accepted 24 April 1984

Publication Date:
19 July 2018 (online)

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Summary

Clotting enzyme activity was detected in lysates prepared from the coelomocytes of Asterias forbesi following incubation with endotoxin-activated Limulus amebocyte lysate. This activity was not detected in the cell-free coelomic fluid. The enzymatic activity from the sea star lysate hydrolyzed the synthetic substrate S2222 but not S2238 or S2251, and polymerized partially purified Limulus clottable protein. The clotting enzyme activity was not detected following treatment of the sea star cell lysate with endotoxin or with the clotting enzyme from Limulus lysate. The enzymatic activity, generated in sea star cell lysate by the activated Limulus lysate, was inhibited by the addition of benzamidine; and its effect was suppressed with rabbit anti-sera directed against Asterias whole cell lysate, but not with anti-sera directed against the previously reported Sea Star Factor.

Keywords

Clotting enzyme activity - Asterias forbesi - Coelomocyte lysate
 

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