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

Karla Montaño-Pérez; Gloria Yepiz-Plascencia; Inocencio Higuera-Ciapara; Francisco Vargas-Albores

doi:10.1016/S0305-0491(99)00011-5

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

Karla Montaño-Pérez, Gloria Yepiz-Plascencia, Inocencio Higuera-Ciapara, Francisco Vargas-Albores

Centro de Investigacion en Alimentacion y Desarrollo

Research output: Contribution to journal › Article › peer-review

41 Scopus citations

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.

Original language	English
Pages (from-to)	381-387
Number of pages	7
Journal	Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Volume	122
Issue number	4
DOIs	https://doi.org/10.1016/S0305-0491(99)00011-5
State	Published - 1 Jan 1999
Externally published	Yes

Keywords

Clotting protein
Coagulogen
Crustacea
Defense system
Hemocyte lysate
Invertebrate coagulation
Shrimp immunity
Transglutaminase

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10.1016/S0305-0491(99)00011-5

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title = "Purification and characterization of the clotting protein from the white shrimp Penaeus vannamei",

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.",

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Purification and characterization of the clotting protein from the white shrimp Penaeus vannamei. / Montaño-Pérez, Karla; Yepiz-Plascencia, Gloria; Higuera-Ciapara, Inocencio et al.
In: Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology, Vol. 122, No. 4, 01.01.1999, p. 381-387.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Purification and characterization of the clotting protein from the white shrimp Penaeus vannamei

AU - Montaño-Pérez, Karla

AU - Yepiz-Plascencia, Gloria

AU - Higuera-Ciapara, Inocencio

AU - Vargas-Albores, Francisco

PY - 1999/1/1

Y1 - 1999/1/1

N2 - 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.

AB - 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.

KW - Clotting protein

KW - Coagulogen

KW - Crustacea

KW - Defense system

KW - Hemocyte lysate

KW - Invertebrate coagulation

KW - Shrimp immunity

KW - Transglutaminase

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M3 - Artículo

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SN - 0305-0491

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JO - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology

JF - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology

IS - 4

ER -

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

Abstract

Keywords

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