Isolation and characterization of a fish F-type lectin from gilt head bream (Sparus aurata) serum

Nicolo' Parrinello, Matteo Cammarata, Aiti Vizzini, Giuseppina Salerno, Gerardo R. Vasta, Eric W. Odom, Gigliola Benenati

Risultato della ricerca: Article

38 Citazioni (Scopus)

Abstract

A novel fucose-binding lectin, designated SauFBP32, was purified by affinity chromatography on fucose-agarose, from the serum of the gilt head bream Sparus aurata. Electrophoretic mobility of the subunit revealed apparent molecular weights of 35 and 30 kDa under reducing and non-reducing conditions, respectively. Size exclusion analysis suggests that the native lectin is a monomer under the selected experimental conditions. Agglutinating activity towards rabbit erythrocytes was not significantly modified by addition of calcium or EDTA; activity was optimal at 37 degrees C, retained partial activity by treatment at 70 degrees C, and was fully inactivated at 90 degrees C. On western blot analysis, SauFBP showed intense cross-reactivity with antibodies specific for a sea bass (Dicentrarchus labrax) fucose-binding lectin. In addition, the similarity of the N-terminal sequence and a partial coding domain to teleost F-type lectins suggests that SauFBP32 is a member of this emerging family of lectins.
Lingua originaleEnglish
pagine (da-a)150-155
Numero di pagine6
RivistaBIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
Volume1770
Stato di pubblicazionePublished - 2007

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All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology

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