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^*

^*Autore corrispondente per questo lavoro

Centro de Investigacion en Alimentacion y Desarrollo

Risultato della ricerca › peer review

41 Citazioni (Scopus)

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.

Lingua originale	English
pagine (da-a)	381-387
Numero di pagine	7
Rivista	Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Volume	122
Numero di pubblicazione	4
DOI	https://doi.org/10.1016/S0305-0491(99)00011-5
Stato di pubblicazione	Published - 1 gen 1999
Pubblicato esternamente	Sì

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10.1016/S0305-0491(99)00011-5

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https://www.scopus.com/pages/publications/0032901073

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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.",

keywords = "Clotting protein, Coagulogen, Crustacea, Defense system, Hemocyte lysate, Invertebrate coagulation, Shrimp immunity, Transglutaminase",

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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

UR - https://www.scopus.com/pages/publications/0032901073

U2 - 10.1016/S0305-0491(99)00011-5

DO - 10.1016/S0305-0491(99)00011-5

M3 - Artículo

AN - SCOPUS:0032901073

SN - 0305-0491

VL - 122

SP - 381

EP - 387

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

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