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: Article

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

Huella dactilar

Monophenol Monooxygenase
Bivalvia
Agaricales
Polymerization
Dihydroxyphenylalanine
Proteins
Mytilus edulis
Amino Acids
Staphylococcal Protein A
Electrophoresis
Urea
Polyacrylamide Gel Electrophoresis
Derivatives
Molecules
Acids
In Vitro Techniques

ASJC Scopus subject areas

  • Physiology
  • Biochemistry
  • Molecular Biology

Citar esto

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title = "In vitro polymerization of mussel polyphenolic proteins catalyzed by mushroom tyrosinase",
abstract = "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.",
keywords = "Adhesive proteins, Byssus, Catechol oxidase, Cross- linking, Dopa, Mussel, Polyphenolic protein, Sclerotization, Tyrosinase",
author = "Burzio, {Luis A.} and Burzio, {Veronica A.} and Joel Pardo and Burzio, {Luis O.}",
year = "2000",
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In vitro polymerization of mussel polyphenolic proteins catalyzed by mushroom tyrosinase. / Burzio, Luis A.; Burzio, Veronica A.; Pardo, Joel; Burzio, Luis O.

En: Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology, Vol. 126, N.º 3, 30.08.2000, p. 383-389.

Resultado de la investigación: Article

TY - JOUR

T1 - In vitro polymerization of mussel polyphenolic proteins catalyzed by mushroom tyrosinase

AU - Burzio, Luis A.

AU - Burzio, Veronica A.

AU - Pardo, Joel

AU - Burzio, Luis O.

PY - 2000/8/30

Y1 - 2000/8/30

N2 - 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.

AB - 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.

KW - Adhesive proteins

KW - Byssus

KW - Catechol oxidase

KW - Cross- linking

KW - Dopa

KW - Mussel

KW - Polyphenolic protein

KW - Sclerotization

KW - Tyrosinase

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U2 - 10.1016/S0305-0491(00)00188-7

DO - 10.1016/S0305-0491(00)00188-7

M3 - Article

C2 - 11007180

AN - SCOPUS:0033868917

VL - 126

SP - 383

EP - 389

JO - Comparative biochemistry and physiology. B, Comparative biochemistry

JF - Comparative biochemistry and physiology. B, Comparative biochemistry

SN - 1096-4959

IS - 3

ER -