Determination of the N-glycosylation patterns of seed proteins: applications to determine the authenticity and substantial equivalence of genetically modified (GM) crops

J Agric Food Chem. 2011 Aug 24;59(16):8779-88. doi: 10.1021/jf2010854. Epub 2011 Aug 3.

Abstract

Methods have been developed to determine the N-glycosylation pattern of proteins at the single-seed level in two different biological systems. These were the well-characterized and widely consumed storage protein phaseolin from several species of Phaseolus (bean) and the α-amylase inhibitor from the same Phaseolus species expressed transgenically in pea. The N-glycosylation pattern of the α-amylase inhibitor expressed transgenically in pea was different from that of the inhibitor present in common bean (P. vulgaris), the species of origin of the gene. However, multivariate analysis showed that the differences in N-glycan patterns between the α-amylase inhibitors from common bean and pea were less than those between the inhibitors from common bean and two related bean species, lima bean (Phaseolus lunatus) and tepary bean (Phaseolus acutifolius).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Glycosylation
  • Pisum sativum / chemistry
  • Pisum sativum / genetics
  • Plant Lectins / chemistry
  • Plant Lectins / genetics
  • Plant Proteins / chemistry*
  • Plant Proteins / genetics
  • Plants, Genetically Modified / chemistry
  • Plants, Genetically Modified / classification*
  • Seeds / chemistry*
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Substances

  • Plant Lectins
  • Plant Proteins
  • alpha-amylase inhibitor, Phaseolus vulgaris
  • phaseolin protein, Phaseolus vulgaris