1979
DOI: 10.1002/jsfa.2740300112
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Extraction and fractionation of wheat flour proteins

Abstract: Extraction of wheat flour with 1.5 % sodium dodecyl sulphate (SDS) solution dissolved 65-67 % of the total flour nitrogen. The SDS-insoluble proteinaceous material was separated into glycoproteins-I, I1 and I11 by ultracentrifugation. Part of the SDSsoluble proteinaceous material was precipitated by addition of ethanol and separated into glycoproteins-IV, glutenins and globulins. The rest of the dissolved proteinaceous material was separated into glycoproteins-V, gliadins, glycoproteins-VI, and albumins by (NH… Show more

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Cited by 62 publications
(50 citation statements)
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“…This can be attributed to SDS-induced unfolding of the protein chains. In general, by disrupting hydrophobic interactions in proteins, SDS separates polypeptide chains into 'rod-shaped' units (Graveland et al, 1979). Therefore, the greater E could have resulted from a more linear orientation of protein molecules in SPI films containing SDS.…”
Section: Tensile Propertiesmentioning
confidence: 99%
See 1 more Smart Citation
“…This can be attributed to SDS-induced unfolding of the protein chains. In general, by disrupting hydrophobic interactions in proteins, SDS separates polypeptide chains into 'rod-shaped' units (Graveland et al, 1979). Therefore, the greater E could have resulted from a more linear orientation of protein molecules in SPI films containing SDS.…”
Section: Tensile Propertiesmentioning
confidence: 99%
“…Such treatments mainly promote cross-linking within the protein film network. Ionic surfactants, such as sodium dodecyl sulfate (SDS), are powerful denaturing and dissociating agents for proteins (Graveland et al, 1979;Cheftel et al, 1985). Strength reduction, and even re-solubilization, of protein gels in SDS buffers has been reported (Kitabatake and Doi, 1993;McClements et al, 1993;Kiosseoglou et al, 1999).…”
Section: Introductionmentioning
confidence: 99%
“…The definition of different classes of wheat proteins has been made according to the solubility and is by no means chemically strict [24]. Thus, it is possible that the gliadin preparation used in the present study also includes some contami nation from salt-soluble albumins or globulins, which in SDS-PAGE are localized below 20 kd and between 20 and 90 kd, respectively [25]. IgG-class antibodies against glutenin, subfractions of gliadin, wheat albu mins and globulins, measured by ELISA and immunofluroescent technique, have been reported in the sera of both GSE patients and healthy controls [24,26].…”
Section: Discussionmentioning
confidence: 99%
“…Three patients had no IgA antibodies, 1 of these had IgA de ficiency. With the remaining 4 GSE sera, in addition to the staining of the same major bands with both iso types, IgG staining of 1-5 polypeptides of those with MW of 14,15,16,17,19,20,25,26,53, 60 and 68 kd was seen.…”
Section: Comparison Of a G A Pattern To Jejunal Morphologymentioning
confidence: 99%
“…Z rozdziału chromatograficznego w kolumnach HPSEC (wyników nie zamieszczono) wynika, że objętość elucji albuminy pokrywała się z objętością elucji wzorcowej albuminy woło-wej, o masie cząsteczkowej 6,6 × 10 4 g/mol i mieściła się w zakresie zmienności podanym w literaturze, charakterystycznym dla albuminy pszenicy, wyznaczonym techniką SEC [11] i żyta, oznaczonym techniką SDS Page [21].…”
Section: Właściwości Białka Rozpuszczalnego (Albuminy) Oraz Nierozpusunclassified