Characterization of Oat Vicilin-Like Polypeptides | Zendy

Khosrow Adeli | Zendy; Illimar Altosaar | Zendy

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Characterization of Oat Vicilin-Like Polypeptides

Author(s) -

Khosrow Adeli,

Illimar Altosaar

Publication year - 1984

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.75.1.225

Subject(s) - vicilin , avena , globulin , legumin , legume , storage protein , gel electrophoresis , polyacrylamide gel electrophoresis , biochemistry , sodium dodecyl sulfate , pisum , biology , glycoprotein , glycine , chemistry , chromatography , botany , amino acid , gene , immunology , enzyme

The 7S and 3S globulin fractions were extracted and characterized from Avena sativa L. seeds which showed similar solubility characteristics and holoprotein size to those of the vicilin fraction in legumes. These holoproteins were characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, isoelectrofocussing, and two-dimensional electrophoresis. Among the components of the oat reserve globulins, the 7S fraction was capable of binding to concanavalin A-Sepharose, thus indicating it to be a glycoprotein. This pattern of the glycosylation of the reserve proteins in oat resembles that observed in certain legume seeds such as Pisum sativum and Glycine max. The results support the notion that the protein components of cereal and legume globulins may be homologous.

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