Accumulation of Gliadin and Glutenin Polypeptides during Development of Normal and Sulphur-deficient Wheat Seed: Analysis using Specific Monoclonal Antibodies

Skerritt, John H.; Lew, Patricia Y.; Castle, SL

doi:10.1093/jxb/39.6.723

Cited by 21 publications

(10 citation statements)

References 31 publications

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“…Grimwade et al (1996) reported that mRNAs for the various groups of gluten proteins were detected from 11 days after anthesis, and the proteins were detected from about 14 days after anthesis. When using acidic-polyacrylamide gel electrophoresis (A-PAGE), the gliadin bands became visible at about 6 days (Greene et al, 1985), 10 days (Bartels and Thompson, 1986;Johansson et al, 1994;Ng et al, 1990), 8 -12 days (Skerritt et al, 1988), and 12 -15 days (Mecham et al, 1981) after anthesis. The glutenin banding patterns on sodium dodecylsulfate-PAGE (SDS-PAGE) were detectable at 8 days (Skerritt et al, 1988), 10 days (Bartels and Thompson, 1986;Shewry et al, 2009), 13 days (Ng et al, 1990), and 14 days (Johansson et al, 1994) after anthesis.…”

Section: Methodsmentioning

confidence: 99%

“…When using acidic-polyacrylamide gel electrophoresis (A-PAGE), the gliadin bands became visible at about 6 days (Greene et al, 1985), 10 days (Bartels and Thompson, 1986;Johansson et al, 1994;Ng et al, 1990), 8 -12 days (Skerritt et al, 1988), and 12 -15 days (Mecham et al, 1981) after anthesis. The glutenin banding patterns on sodium dodecylsulfate-PAGE (SDS-PAGE) were detectable at 8 days (Skerritt et al, 1988), 10 days (Bartels and Thompson, 1986;Shewry et al, 2009), 13 days (Ng et al, 1990), and 14 days (Johansson et al, 1994) after anthesis. Further studies using a reversedphase high-performance liquid chromatography (RP-HPLC) technique detected small quantities of the gliadin and glutenin monomers in the early stages of kernel development, but the bulk of these proteins were synthesized in later stages of development.…”

Section: Methodsmentioning

confidence: 99%

“…As described above, several authors have studied compositional changes in gluten proteins during kernel development (Abonyi et al, 2007;Bartels and Thompson, 1986;Greene et al, 1985;Grimwade et al, 1996;Iametti et al, 2006;Johansson et al, 1994;Mecham et al, 1981;Ng et al, 1990;Skerritt et al, 1988). However, relatively few studies have examined individual gluten proteins at the subunit level.…”

Section: Introductionmentioning

confidence: 99%

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Expression and Development of Wheat Proteins during Maturation of Wheat Kernel and the Rheological Properties of Dough Prepared from the Flour of Mature and Immature Wheat

Katagiri¹,

Masuda²,

Tani³

et al. 2011

FSTR

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Changes in expression and accumulation of gluten proteins were investigated in developing kernels of 2 wheat cultivars, Norin 61 and Fukusayaka. Expression of 7 gluten subunit genes was detectable 7 days after anthesis (DAA) in both cultivars, while changes in expression patterns of these subunits over time were found to be specific to each cultivar. The accumulation of total proteins and ethanol-soluble proteins was analysed by SDS-PAGE and acidic-PAGE, respectively. The band patterns of total proteins in both cultivars changed markedly between 14 and 21 DAA. Ethanol-soluble proteins, which are mainly gliadin proteins, were detected at 21 DAA in Norin 61 and at 14 DAA in Fukusayaka. We investigated the textural properties of dough prepared from the flour of mature and immature Norin 61. The tension test revealed that dough prepared from immature wheat had higher tensile strength and lower extensibility than that prepared from mature wheat.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Expression and Development of Wheat Proteins during Maturation of Wheat Kernel and the Rheological Properties of Dough Prepared from the Flour of Mature and Immature Wheat

Katagiri¹,

Masuda²,

Tani³

et al. 2011

FSTR

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“…Some of the gluten-specific ELISA kits, such as the Morinaga Wheat Gliadin kit (Morinaga Institute of Biological Science, Japan), use polyclonal antibodies (pAb) while other tests were developed using monoclonal antibodies (mAb) e.g. Skerritt antibody, specific for omega gliadins and HMW glutenins (Skerritt et al 1988) coupled with different extraction methods and calibration materials. Enhanced detection of toxic peptides can be carried out by the use of mAbs raised against known immunoreactive epitopes.…”

Section: Introductionmentioning

confidence: 99%

Celiac disease-specific prolamin peptide content of wheat relatives and wild species determined by ELISA assays and bioinformatics analyses

Gell¹,

Kovács²,

Molnár³

et al. 2015

Cereal Research Communications

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Enzyme-linked immunosorbent assays (ELISAs) are widely used to determine gluten contamination in gluten-free and low gluten food samples. ELISA assays developed using monoclonal antibodies against known toxic peptides have an advantage in the identification of toxic prolamin content in protein extracts of different food samples, as well as raw materials. R5 and G12 monoclonal antibodies specific for two known toxic peptides used in commercially available gluten ELISA assays were applied to test toxic peptide contents in wheat relatives and wild wheat species with different genome composition and complexity. Although the R5 peptide content showed some correlation with ploidy levels in Triticum species, there was a high variance among Aegilops species. Some of the analysed diploid Aegilops species showed extremely high R5 peptide contents. Based on the bioinformatics analyses, the R5 peptide was present in most of the sulphur rich prolamins in all the analysed species, whereas the G12 epitope was exclusively present in alpha gliadins. High variation was detected in the position and frequency of epitopes in sequences originating from the same species, thus highlighting the importance of genotypic variation within species. Identification of new prolamin alleles of wheat relatives and wild wheat species is of great importance in order to find germplasm for special end-use quality purposes as well as development of food with reduced toxicity.

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“…The gluten proteins are accumulated in the grain in order to store nitrogen and sulphur for the germination. Although the exact dpa at which the grain starts to accumulate the gluten proteins is difficult to define, and depends on the technique used to detect them, the gluten proteins have already been found in the grain after a few dpa 16. The difference between wheat varieties for bread‐making purposes may thus already exist at an early stage of grain development.…”

mentioning

confidence: 99%

Early prediction of wheat quality: analysis during grain development using mass spectrometry and multivariate data analysis

Ghirardo

Sørensen

Petersen

et al. 2005

Rapid Comm Mass Spectrometry

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Matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry and multivariate data analysis have been used for the determination of wheat quality at different stages of grain development. Wheat varieties with one of two different end-use qualities (i.e. suitable or not suitable for bread-making purposes) were investigated. The samples were collected from grains from 15 until 45 days post-anthesis (dpa). Gluten proteins from wheat grains were extracted and subsequently analysed by mass spectrometry. Discrimination partial least-squares regression and soft independent modelling of class analogy were used to determine the quality of new and unknown wheat samples. With these methods, we were able to predict correctly the end-use qualities at every stage investigated. This new fast technique, based on the rapidity of mass spectrometry combined with the objectivity of multivariate data analysis, offers a method that can replace the traditional rather time-consuming ones such as gel electrophoresis. This study focused on the determination of wheat quality at 15 dpa, when the grain is due for harvest 1 month later.

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Accumulation of Gliadin and Glutenin Polypeptides during Development of Normal and Sulphur-deficient Wheat Seed: Analysis using Specific Monoclonal Antibodies

Cited by 21 publications

References 31 publications

Expression and Development of Wheat Proteins during Maturation of Wheat Kernel and the Rheological Properties of Dough Prepared from the Flour of Mature and Immature Wheat

Expression and Development of Wheat Proteins during Maturation of Wheat Kernel and the Rheological Properties of Dough Prepared from the Flour of Mature and Immature Wheat

Celiac disease-specific prolamin peptide content of wheat relatives and wild species determined by ELISA assays and bioinformatics analyses

Early prediction of wheat quality: analysis during grain development using mass spectrometry and multivariate data analysis

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