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Inhibition of Lysinoalanine Synthesis by Protein Acylation

  • Mendel Friedman
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 105)

Abstract

Treating wheat gluten, soy protein, and lactalbumin under alkaline conditions at 65°C for various times destroys part of the threonine, cystine, lysine, tyrosine, and arginine residues in these proteins. The losses were accompanied by the appearance of lysinoalanine and unidentified ninhydrin-positive substances. Treating wool under samewhat milder alkaline conditions destroys part of the cystine and lysine residues, but not the other amino acids cited. In this case, loss of cystine and lysine was accompanied by the appearance of lanthionine and lysinoalanine. Amino acid analysis of alkali-treated acylated proteins revealed that acylation by acetic and succinic anhydrides prevents or minimizes destruction of lysine residues and the formation of lysinoalanine in wheat gluten and soy protein and, in wool, minimizes destruction of cystine and lysine residues and the formation of lanthionine lysinoalanine. Mechanisms are proposed to explain the observed inhibiting effects of protein acylation and certain additives on lysinoalanine formation.

Keywords

Amino Acid Composition Lysine Residue Acetic Anhydride Amino Acid Analysis Alkali Treatment 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1978

Authors and Affiliations

  • Mendel Friedman
    • 1
  1. 1.U.S. Department of AgricultureWestern Regional Research LaboratoryBerkeleyUSA

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