Journal of Lipid Research, Vol. 8, 609-614, November 1967
Copyright © 1967 by Lipid Research, Inc.

Interaction of phospholipid-metal complexes with water-soluble wheat protein

J. G. Fullington

Western Regional Research Laboratory, Agricultural Research Service, U. S. Department of Agriculture, Albany, California 94710

Insoluble lipid-protein complexes are formed in the presence of Ni(II), Ca(II), or Mg(II) by specific components of the water-soluble proteins of wheat flour and either triphosphoinositide or phosphatidyl serine. The pattern of protein species bound by the lipid-metal complex is dependent upon the metal and the phospholipid used. A group of proteins, containing carbohydrate, may be solubilized and recovered by washing the precipitate with acidic chloroform-methanol-water.

Analyses of reactive and nonreactive protein species have shown no differences which clearly account for their behavior. Methylation of protein increases binding to lipid; acetylation decreases the interaction. Weak interaction has been observed between certain components of flour proteins and phospholipid in the absence of metal ions, but the components differ from those bound in the presence of metal ions.

It is suggested that properly oriented groups of the protein molecules are chelating onto available coordination positions of metal ions already bound to phospholipid.

Supplementary key words complexes • Ni(II), Ca(II), Mg(II) • soluble proteins • triphosphoinositide • phosphatidyl serine • oriented groups • coordination

Submitted on April 25, 1967
Accepted on August 7, 1967

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