Plant Foods for Human Nutrition

, Volume 54, Issue 2, pp 93–100

Agglutinating activity of alcohol-soluble proteins from quinoa seed flour in celiac disease

Authors

  • M. De Vincenzi
    • Laboratorio AlimentiIstituto Superiore di Sanità
  • M. Silano
    • Clinica PediatricaOspedale S.Paolo, Università di Milano
  • R. Luchetti
    • Laboratorio AlimentiIstituto Superiore di Sanità
  • B. Carratù
    • Laboratorio AlimentiIstituto Superiore di Sanità
  • C. Boniglia
    • Laboratorio AlimentiIstituto Superiore di Sanità
  • N.E. Pogna
    • Istituto Sperimentale Cerealicoltura
Article

DOI: 10.1023/A:1008059519025

Cite this article as:
De Vincenzi, M., Silano, M., Luchetti, R. et al. Plant Foods Hum Nutr (1999) 54: 93. doi:10.1023/A:1008059519025

Abstract

The edible seeds of the quinoa plant contain small quantities of alcohol-soluble protein which, after peptic-tryptic digestion, are unable to agglutinate K562(s) cells. When separated by affinity chromatography on sepharose-6B coupled with mannan, peptic-tryptic digest separated in two fractions. Fraction B peptides (about 1% of total protein) were shown to agglutinate K562(s) cells at a very low concentration, whereas peptides in fraction A and in the mixed fraction A+B were inactive, suggesting that fraction A contains protective peptides that interfere with the agglutinating activity of toxic peptides in fraction B.

Amino acidsCeliac diseaseCellsCerealsProlaminesQuinoa seeds

Copyright information

© Kluwer Academic Publishers 1999