Recently we reported that removal of noncovalently bonded protein from glutenin resulted in decreased viscoelasticity. In that study, two glutenin fractions were isolated by successive gel filtration of glutenin on Sephadex G-200 in the solvents acetic acid-guanidine hydrochloride (GuHCl)-cetyltrimethylammonium bromide (AGC) and sodium dodecyl sulfate (SDS). This note reports the S20,W values o...

Genetic and environmental factors that affect the formation of glutenin macropolymer (GMP) particles were investigated by growing Lance 5C 10, Lance 2C12, Warigal 5C10 and Warigal 2C12 lines under widely differing temperature regimes in greenhouse conditions. The GMP characteristics and mixing properties of flour extracted from mature wheat kernels were systematically studied. The amount of GMP...

Glutenin is a major protein fraction contributing to the functional properties of gluten and dough. The glutenin constitutes 30-40% of the protein in wheat flour and about half of that in gluten. It is essential to identify correct glutenin alleles and to improve wheat quality by selecting alleles that exert favorable effects. Moroccan wheat cultivars are unique in West Asia and North Africa re...

Wheat omega-5 gliadin and a high m.w. glutenin subunit (HMW-glutenin) have been reported as major allergens in wheat-dependent exercise-induced anaphylaxis. A simultaneous detection of specific IgE to epitope sequences of both proteins is considered to be a reliable method for diagnosis of wheat-dependent exercise-induced anaphylaxis. However, the IgE-binding epitope of HMW-glutenin remains unk...

The influence of various solvents upon the conformation of gluten proteins, glutenin and gliadin, has been studied by optical rotatory dispersion (ORD), circular dichroism (CD), and infrared (lR) absorption measurements. From ORD data an alpha-helix content of 38% has been calculated for gliadin in trifluoroethanol; 35% for glutenin. Conversely, little or no alpha-helix was found when the prote...

Abstract Background Wheat flour maturation affects the aggregation and structural stability of proteins. The number high-molecular-weight glutenin subunits (HMW-GSs) differs in various wheat varieties. effects Dx2 absence on protein characteristics thermal were investigated during 120 days using near-isogenic lines (NILs). Results delayed decreased flours maturation, i.e., maturation-induced in...

Gliadin and glutenin were examined to identify peptides that differentiate the proteins. Pronase-resistant fragments from gliadin and glutenin have average molecular weights of 460 and 640, respectively, and in acid are readily converted to pyroglutamic acid (PGA) peptides. PGA-peptides isolated from pepsin-hydrolyzed Pronase digests contained glutamine (Gin) or glutamic acid; proline, serine, ...

Six commercial U.K. cultivars of winter wheat selected to represent different abilities to partition nitrogen into grain protein were grown in replicated field trials at five different sites over three seasons. The proportion of LMW glutenin subunits decreased and the proportion of gliadins increased during grain development and in response to N application. Differences were observed between th...

The expression of a wheat genomic clone containing the entire coding sequence of the high molecular weight glutenin subunit 12 gene flanked by 2.6 kilobases of 5' and 1.5 kilobases of 3' sequences has been studied after introduction into tobacco. Seeds of different tobacco plants containing the full-length wheat genomic clone accumulated different amounts of intact high molecular weight gluteni...