Electrophoretic Characterization of Quinoa Seed Proteins

Abstract

Quinoa (Chenopodium quinoa Willd) is an important domesticated food crop of the Andean highlands with potential as an alternative crop elsewhere. Among its most attractive characteristics are the quantity and favorable amino acid balance of the seed proteins. The objective of this study was to characterize quinoa seed proteins by electrophoretic mobility, solubility fractionation, and genetic variability from a wide genetic base. Electrophoretic profiles of denatured albumin, globulin, prolamin, and glutelin solubility fractions demonstrated that quinoa seed polypeptides could be classified as either albumin or globulin with most predominant polypeptides in the globulin fraction. Insignificant amounts of protein were present in the prolamin fraction and all polypeptides in the glutelin fraction had identical electrophoretic mobilities to albumins and globulins. Three globulin polypeptides of 34.3, 35.6, and 36.2 kilodaltons in size were highly variable within and among the accessions examined and appear to be coded by at least two loci. Two‐dimensional peptide mapping revealed that these three polypeptides were homologous. These highly variable markers could be used for identification and classification of germplasm and elucidation of systematics and genetic variability within the quinoa germplasm pool. All other major polypeptides were electrophoretically invariant among the accessions examined. Copyright © 1990, Wiley Blackwell. All rights reserved