Purification and characterization of the clotting protein from the white shrimp Penaeus 6annamei

Tipo de material: Texto

TextoSeries ; Comparative BioChemistry and Physiology, 122B, p.381-387, 1999Trabajos contenidos:

Montano-Pérez, K
Yepiz-Plascencia, G
Higuera-Ciapara, I
Vargas-Albores, F

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Resumen: 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.

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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.

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