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Purification and characterization of the clotting protein from the white shrimp Penaeus vannamei

*Corresponding author for this work
  • Centro de Investigacion en Alimentacion y Desarrollo
Research Output:
Contribution to journal
Article
Peer-review

Publication Information

Output type

Research Output:
Contribution to journal
Article
Peer-review

Original language

English

Pages from-to (Number of pages)

Pages 381-387 (7 pages)

Journal (Volume, Issue Number)

Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology (Volume 122, Issue 4)

Publication milestones

  • Published - 01/01/1999

Publication status

Published - 01/01/1999

ISSN

0305-0491

Publication IDs

  • Scopus: 0032901073

Abstract

The protein responsible for clot formation was isolated from plasma of the white shrimp Penaeus vannamei 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. Copyright (C) 1999 Elsevier Science Inc.