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Purification of hemocyanin from white shrimp (Penaeus vannamei boone) by immobilized metal affinity chromatography

  • Ciria G. Figueroa-Sotoa(Author)
    ,
  • Ana Maria Calderón De La Barcaa(Author)
    ,
  • Luz Vazquez-Morenoa(Author)
    ,
  • Inocencio Higuera-Ciaparaa(Author)
    ,
  • Gloria Yepiz-Plascenciaa(Author)
  • aCentro 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 203-208 (6 pages)

Journal (Volume, Issue Number)

Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology (Volume 117, Issue 2)

Publication milestones

  • Published - 01/01/1997

Publication status

Published - 01/01/1997

ISSN

0305-0491

External Publication IDs

  • Scopus: 0030805082

Abstract

Hemocyanin (Hc) was isolated from white shrimp (Penaeus vannamei Boone) plasma by density gradient ultracentrifugation and immobilized metal affinity chromatography. Hc was contained in the subnatant high density fraction and was adsorbed by an iminodiacetic acid (Ni-DA) column that bound Hc and apohemocyanin. Hc molecular weight was estimated by pore limiting electrophoresis as 400 kDa. It is composed of two subunits of approximately 75 and 82 kDa. This 400-kDa protein contained copper and was detected by antibodies raised against the purified subunitsl Isoelectric points of the affinity purified native protein were 4.8 and 4.9. Presence of covalently bound carbohydrates in both subunits was detected by biotinylated lectins and avidinhorseradish peroxidase.

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