Heterogeneity of wheat endosperm proteolipids (CM proteins)

Rodriguez Loperena, M.A. and Aragoncillo Ballesteros, Cipriano and Carbonero Zalduegui, Pilar and García Olmedo, Francisco (1975). Heterogeneity of wheat endosperm proteolipids (CM proteins). "Phytochemistry", v. 14 (n. 5-6); pp. 1219-1223. ISSN 0031-9422. https://doi.org/10.1016/S0031-9422(00)98598-4.

Description

Title: Heterogeneity of wheat endosperm proteolipids (CM proteins)
Author/s:
  • Rodriguez Loperena, M.A.
  • Aragoncillo Ballesteros, Cipriano
  • Carbonero Zalduegui, Pilar
  • García Olmedo, Francisco
Item Type: Article
Título de Revista/Publicación: Phytochemistry
Date: June 1975
ISSN: 0031-9422
Volume: 14
Subjects:
Freetext Keywords: Triticum aestivum; Triticum durum; Aegilops squarrosa; Gramineae; wheat; proteolipids; CM proteins; gliadins; albumins; electrofocusing; electrophoresis
Faculty: E.T.S.I. Agrónomos (UPM) [antigua denominación]
Department: Biotecnologia [hasta 2014]
Creative Commons Licenses: Recognition - No derivative works - Non commercial

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Abstract

Proteins extracted with CHCl3-MeOH from wheat endosperm have been fractionated by Sephadex G-100 and the 15 000–20 000 MW range fraction, designated CM protein, has been examined by combined electrofocusing (pH range 5–8) and electrophoresis (pH 3.2) and the heterogeneity of the electrophoretic components has been ascertained. It has been shown by joint mapping and by sequential extraction that CM proteins are extracted by 70% EtOH but not by H2O, although they can be made water-soluble after dialysis against an acid buffer, pH 3.2, 3 M urea, without losing their solubility in CHCl3-MeOH mixtures. It is concluded that CM proteins fit the definition of a Folch—Lees proteolipid. The Triticum aestivum (genomes ABD) map can be reconstructed by mixing T. durum (AB) and Aegilops squarrosa (D). The low intragenomic variability of CM protein is confirmed.

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