Thromb Haemost 1981; 45(01): 077-081
DOI: 10.1055/s-0038-1650133
Original Article
Schattauer GmbH Stuttgart

Purification and Characterization of the Sand Crab (Ovalipes bipustulatus) Coagulogen (Fibrinogen)

F Madaras
The Department of Haematology, Repatriation General Hospital, Department of Veterans' Affairs, Heidelberg West, Victoria, Australia
,
M Y Chew
The Department of Haematology, Repatriation General Hospital, Department of Veterans' Affairs, Heidelberg West, Victoria, Australia
,
J D Parkin
The Department of Haematology, Repatriation General Hospital, Department of Veterans' Affairs, Heidelberg West, Victoria, Australia
› Author Affiliations
Further Information

Publication History

Received 17 April 1980

Accepted after revision 22 December 1980

Publication Date:
04 July 2018 (online)

Summary

From the coagulocytes (amoebocytes) coagulogen (fibrinogen) was isolated, and purified on Sephacryl S-200.

The cell homogenate contained one major protein species with a minimum molecular weight of 70,000. This protein clotted in the presence of human thrombin, human factor XIII and Ca++.

The coagulogen contained no free thiol groups, however these were detectable in the reduced protein. Using the cyanoethylation procedure, it was estimated that one coagulogen molecule contained two lysine residues which participated in the cross-linking reaction. The total amino add composition of the crab coagulogen and coagulin (fibrin) was estimated and compared with the amino acid composition of the Limulus polyphemus, lobster (Panulirus interruptus) and porcine fibrinogen.

 
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