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

  • Ciria G. Figueroa-Soto
  • , Ana Maria Calderón De La Barca
  • , Luz Vazquez-Moreno
  • , Inocencio Higuera-Ciapara
  • , Gloria Yepiz-Plascencia*
  • *Autore corrispondente per questo lavoro

Risultato della ricercapeer review

25 Citazioni (Scopus)

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.

Lingua originaleEnglish
pagine (da-a)203-208
Numero di pagine6
RivistaComparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Volume117
Numero di pubblicazione2
DOI
Stato di pubblicazionePublished - 1 gen 1997
Pubblicato esternamente

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