title: The wide diversity of structurally similar wine proteins.
abstract: In the present work, single grape variety wines, Moscatel and Arinto, were used. Analysis by denaturing polyacrylamide gel electrophoresis of the wine proteins revealed the presence of only a few polypeptides ranging in molecular mass from 15 to 30 kDa. However, a more detailed examination of the whole protein fraction, by a combination of techniques, showed that these wines contain a very large number (many tens and, possibly, many more) of distinct polypeptides, exhibiting similar molecular masses but different electrical charges. The results obtained using highly specific antibodies and N-terminal sequencing indicate that there is structural similarity among most of the wine polypeptides. These observations can be explained by the existence of a common precursor to most or all of the wine proteins, which could generate all of the detected polypeptides by limited proteolysis. Comparison of the N-terminal sequences of the polypeptides isolated from Moscatel wine with proteins from other sources revealed a high degree of homology to pathogenesis-related proteins.
authors.affiliation: Instituto Superior de Agronomia, Universidade Técnica de Lisboa, 1349-017 Lisboa, Portugal.
authors.forename: S
authors.initials: S
authors.lastname: Monteiro
authors.forename: M A
authors.initials: MA
authors.lastname: Piçarra-Pereira
authors.forename: P R
authors.initials: PR
authors.lastname: Mesquita
authors.forename: V B
authors.initials: VB
authors.lastname: Loureiro
authors.forename: A
authors.initials: A
authors.lastname: Teixeira
authors.forename: R B
authors.initials: RB
authors.lastname: Ferreira
mesh_terms: D000595:Amino Acid Sequence; D002852:Chromatography, Ion Exchange; D004587:Electrophoresis, Agar Gel; D015151:Immunoblotting; D011506:Proteins / Q000032:analysis / Q000737:chemistry*; D014920:Wine / Q000032:analysis*
chemical_list: D011506:Proteins