Starch gel electrophoresis of wheat gluten proteins with concentrated urea

Woychik, J.H.; Boundy, Joyce A.; Dimler, R. J.

doi:10.1016/0003-9861(61)90075-3

Cited by 255 publications

(69 citation statements)

References 6 publications

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“…Gliadins, which are traditionally classified into three groups (a/b-, g-, and w-gliadins) on the basis of their electrophoretic mobilities on A-PAGE gel (Woychik et al 1961), were extracted from wheat cultivars by A-PAGE (Fig. 1).…”

Section: Identification Of 1bl1rs Translocations By A-pagementioning

confidence: 99%

Fast identification of wheat 1BL.1RS translocation by reversed-phase ultra-performance liquid chromatography (RP-UPLC)

et al. 2013

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Abstract. The 1BL.1RS chromosomal translocation in wheat is the result of replacement of the short arm of chromosome 1B of wheat by the short arm of chromosome 1R of rye, which had been widely used as a parental line in worldwide wheat breeding, resulting in a high percentage of wheat cultivars containing this translocation. A fast and reliable approach to identify this translocation is highly desirable in modern wheat breeding. This study compared reversed-phase ultraperformance liquid chromatography (RP-UPLC), acidic polyacrylamide gel electrophoresis (A-PAGE), liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS), allelic-specific PCR, and reversed-phase highperformance liquid chromatography (RP-HPLC) approaches to identify the 1BL.1RS translocation in 76 bread wheat cultivars. Two gliadin bands in the Gli-B1 region of A-PAGE separation were confirmed by LC-MS/MS to be omega secalins from the 1BL.1RS translocation, and they can be used as reliable protein markers for identifying the translocation. A few specific minor peaks eluted at 12-13 min on the RP-UPLC patterns can readily differentiate the 1BL.1RS translocation. Of the 76 wheat cultivars tested, 40 were identified as carrying the 1BL.1RS translocation by RP-UPLC, which was consistent with the results of A-PAGE, HPLC, and PCR. Compared with other established methods, RP-UPLC showed a clear advantage in fast identification of the 1BL.1RS translocation with higher reliability and lower costs, and it is therefore ideal for large-scale screening of the 1BL.1RS translocation in wheat breeding.

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Section: Identification Of 1bl1rs Translocations By A-pagementioning

confidence: 99%

Fast identification of wheat 1BL.1RS translocation by reversed-phase ultra-performance liquid chromatography (RP-UPLC)

et al. 2013

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“…The major wheat storage proteins are the alcohol-soluble gliadins and the glutenins. The gliadins are monomeric proteins that migrate between Mr 30,000 and 60,000 on SDS-PAGE and are subdivided into a, A, -y, and c gliadins on the basis of fractionation on acidic PAGE (29). A new classification of gliadins into sulfur-rich (a, j3, y) and sulfur-poor (w) fractions was recently suggested (12), based on their amino acid sequence and sulfur content.…”

mentioning

confidence: 99%

Evidence for the Presence of Two Different Types of Protein Bodies in Wheat Endosperm

Rubin

Levanony²,

Galili³

1992

Plant Physiol.

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Storage proteins of wheat grains (Triticum L. em Thell) are deposited in protein bodies inside vacuoles. However, the subcellular sites and mechanisms of their aggregation into protein bodies are not clear. In the present report, we provide evidence for two different types of protein bodies, low-and high-density types that accumulate concurrently and independently in developing wheat endosperm cells. Gliadins were present in both types of protein bodies, whereas the high molecular weight glutenins were localized mainly in the dense ones. Pulse-chase experiments verified that the dense protein bodies were not formed by a gradual increase in density but, presumably, by a distinct, quick process of storage protein aggregation. Subcellular fractionation and electron microscopy studies revealed that the wheat homolog of immunoglobulin heavy-chain-binding protein, an endoplasmic reticulum-resident protein, was present within the dense protein bodies, implying that these were formed by aggregation of storage proteins within the endoplasmic reticulum. The present results suggest that a large part of wheat storage proteins aggregate into protein bodies within the rough endoplasmic reticulum. Because these protein bodies are too large to enter the Golgi, they are likely to be transported directly to vacuoles. This route may operate in concert with the known Golgi-mediated transport to vacuoles in which the storage proteins apparently condense into protein bodies at a postendoplasmic reticulum location. Our results further suggest that although gliadins are transported by either one of these routes, the high molecular weight glutenins use only the Golgi bypass route.

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“…On the basis of the mobilities in low pH gel electrophoresis, the gliadins were initially classified into four groups: α-, β-, γ-, and ω-gliadins, which were in the order of decreasing mobility (Woychik et al, 1961;Wieser, 1996;Wieser, 2007).…”

Section: Classification and Structures Of Gliadinsmentioning

confidence: 99%

Solvent effects on the molecular structures of crude gliadins as revealed by density and ultrasound velocity measurements

Zhang

Scanlon

2011

Journal of Cereal Science

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Starch gel electrophoresis of wheat gluten proteins with concentrated urea

Cited by 255 publications

References 6 publications

Fast identification of wheat 1BL.1RS translocation by reversed-phase ultra-performance liquid chromatography (RP-UPLC)

Fast identification of wheat 1BL.1RS translocation by reversed-phase ultra-performance liquid chromatography (RP-UPLC)

Evidence for the Presence of Two Different Types of Protein Bodies in Wheat Endosperm

Solvent effects on the molecular structures of crude gliadins as revealed by density and ultrasound velocity measurements

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