The adhesive protein of Choromytilus chorus (Molina, 1782) and Aulacomya ater (Molina, 1782): A proline-rich and a glycine-rich polyphenolic protein

Luis A. Burzio, Cristian Saéz, Joel Pardo, J. Herbert Waite, Luis O. Burzio

Resultado de la investigación: Contribución a una revistaArtículorevisión exhaustiva

9 Citas (Scopus)

Resumen

The adhesive polyphenolic proteins from Aulacomya ater and Choromytilus chorus with apparent molecular masses of 135 000 and 105 000, respectively, were digested with trypsin and the peptides produced resolved by reversed phase liquid chromatography. About 5 and 12 major peptides were obtained from the protein of A. ater and C. chorus, respectively. The major peptides were purified by reverse-phase chromatography and the amino acid sequence indicates that both polyphenolic proteins consisted of repeated sequence motifs in their primary structure. The major peptides of A. ater contain seven amino acids corresponding to the consensus sequence AGYGGXK, whereas the tyrosine was always found as 3,4-dihydroxyphenylalanine (Dopa), the X residue in position 6 was either valine, leucine or isoleucine, and the carboxy terminal was either lysine or hydroxylysine. On the other hand, the major peptides of C. chorus ranged in size from 6 to 21 amino acids and the majority correspond to the consensus sequence AKPSKYPTGYKPPVK. Both proteins differ markedly in the sequence of their tryptic peptides, but they share the common characteristics of other adhesive proteins in having a tandem sequence repeat in their primary structure. Copyright (C) 2000 Elsevier Science B.V.

Idioma originalInglés
Páginas (desde-hasta)315-320
Número de páginas6
PublicaciónBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Volumen1479
N.º1-2
DOI
EstadoPublicada - 15 jun. 2000
Publicado de forma externa

Áreas temáticas de ASJC Scopus

  • Biofísica
  • Biología estructural
  • Bioquímica
  • Biología molecular

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