Purification and characterization of the clotting protein from the white shrimp Penaeus 6annamei
Purification and characterization of the clotting protein from the white shrimp Penaeus 6annamei
- Comparative BioChemistry and Physiology, 122B, p.381-387, 1999 .
The protein responsible for clot formation was isolated from plasma of the white shrimp Penaeus 6annamei by affinity chromatography in a heparin-agarose column. The protein, named clotting protein (CP), was found to be a lipoglycoprotein, composed of two 210-kDa subunits covalently bound by disulfide bridges. CP formed large polymers when incubated with hemocyte lysate. Dansylcadaverine can be incorporated into CP by a hemocyte lysate or guinea pig transglutaminase mediated reaction. The amino acid composition and the amino terminal sequence were determined and compared with the clotting protein of the crayfish and the spiny lobster.
DEFENSE SYSTEM
CRUSTACEA
INVERTEBRATE COAGULATION
CLOTTING PROTEIN
SHRIMP IMMUNITY
TRANSGLUTAMINASE
COAGULOGEN
HEMOCYTE LYSATE
The protein responsible for clot formation was isolated from plasma of the white shrimp Penaeus 6annamei by affinity chromatography in a heparin-agarose column. The protein, named clotting protein (CP), was found to be a lipoglycoprotein, composed of two 210-kDa subunits covalently bound by disulfide bridges. CP formed large polymers when incubated with hemocyte lysate. Dansylcadaverine can be incorporated into CP by a hemocyte lysate or guinea pig transglutaminase mediated reaction. The amino acid composition and the amino terminal sequence were determined and compared with the clotting protein of the crayfish and the spiny lobster.
DEFENSE SYSTEM
CRUSTACEA
INVERTEBRATE COAGULATION
CLOTTING PROTEIN
SHRIMP IMMUNITY
TRANSGLUTAMINASE
COAGULOGEN
HEMOCYTE LYSATE