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Blood, Vol. 94 No. 2 (July 15), 1999:
pp. 621-631
Amino Acid Sequence of Trocarin, a Prothrombin Activator From
Tropidechis carinatus Venom: Its Structural Similarity to
Coagulation Factor Xa
Jeremiah S. Joseph,
Maxey C.M. Chung,
Kandiah Jeyaseelan, and
R.
Manjunatha Kini
From the Bioscience Centre, Faculty of Science, the Department of
Biochemistry, Faculty of Medicine, and the Bioprocessing Technology
Centre, Faculty of Engineering, National University of Singapore,
Singapore; and the Department of Biochemistry and Molecular Biophysics,
Medical College of Virginia, Virginia Commonwealth University,
Richmond, VA.
Among snake venom procoagulant proteins, group II prothrombin
activators are functionally similar to blood coagulation factor Xa. We
have purified and partially characterized the enzymatic properties of
trocarin, the group II prothrombin activator from the venom of the
Australian elapid, Tropidechis carinatus (rough-scaled snake).
Prothrombin activation by trocarin is enhanced by Ca2+,
phospholipids, and factor Va, similar to that by factor Xa. However,
its amidolytic activity on peptide substrate S-2222 is significantly lower. We have determined the complete amino acid sequence of trocarin. It is a 46,515-Dalton glycoprotein highly homologous to factor Xa and shares the same domain architecture. The
light chain possesses an N-terminal Gla domain containing 11  -carboxyglutamic acid residues, followed by two epidermal growth
factor (EGF)-like domains; the heavy chain is a serine proteinase. Both
chains are likely glycosylated: the light chain at Ser 52 and the heavy
chain at Asn 45. Unlike other types of venom procoagulants, trocarin is
the first true structural homologue of a coagulation factor. It clots
snake plasma and thus may be similar, if not identical, to snake blood
coagulation factor Xa. Unlike blood factor Xa, it is expressed in high
quantities and in a nonhepatic tissue, making snake venom the richest
source of factor Xa-like proteins. It induces cyanosis and death in
mice at 1 mg/kg body weight. Thus, trocarin acts as a toxin in venom and a similar, if not identical, protein plays a critical role in hemostasis.
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