In vitro polymerization of mussel polyphenolic proteins catalyzed by mushroom tyrosinase

Luis A. Burzio, Veronica A. Burzio, Joel Pardo, Luis O. Burzio

Resultado de la investigación: Contribución a una revistaArtículo

27 Citas (Scopus)

Resumen

The in vitro enzymatic polymerization of the polyphenolic protein purified from the mussels Aulacomya ater, Mytilus edulis chilensis and Choromytilus chorus was studied. Mushroom tyrosinase was used to oxidize the dopa residues present in these proteins, and polymerization was monitored by acid-urea polyacrylamide gel electrophoresis. The protein from A. ater polymerized at a faster rate than the other two. Amino acid analysis of the crosslinked protein showed a notable decrease in the content of dopa, but no significant change of other amino acids. This suggests that crosslink formation may be limited to the oxidized dopa derivatives of the protein molecules. (C) 2000 Elsevier Science Inc.

Idioma originalInglés
Páginas (desde-hasta)383-389
Número de páginas7
PublicaciónComparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Volumen126
N.º3
DOI
EstadoPublicada - 30 ago 2000

Áreas temáticas de ASJC Scopus

  • Fisiología
  • Bioquímica
  • Biología molecular

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