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  • 21
    Electronic Resource
    Electronic Resource
    Barley cultivar discrimination: I. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and glycoprotein blotting (1991)
    Weinheim : Wiley-Blackwell
    Electrophoresis 12 (1991), S. 323-330 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Two different methods of detecting electroblotted glycoproteins after sodium dodecyl sulfate-polyacrylamide gel electrophoresis of Tris-buffer soluble barley seed proteins were examined for their applicability for barley cultivar discrimination. These are the highly specific, lectin-based concanavalin A/peroxidase method and the more general periodate/danyslhydrazine method. The results of the periodate/dansylhydrazine method enabled us to divide the 20 examined cultivars into three groups, whereas the more sensitive concanavalin A/peroxidase method revealed six different glycoprotein patterns. In comparison, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and silver staining of the alcoholsoluble barley seed proteins (hordeins) gave nine different banding patterns. A combination of hordein electrophoresis together with glycoprotein staining by the concanavalin A/peroxidase method made it possible to classify the cultivars into twelve groups, the largest of which contained four cultivars. The qualitative expression of the glycoprotein patterns seemed to be independent of growth conditions, whereas the band intensities obviously were not. As a whole, glycoprotein blotting is a valuable supplement to sodium dodecyl sulfate-polyacrylamide gel electrophoresis of hordeins in barley cultivar discrimination.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150120502
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  • 22
    Electronic Resource
    Electronic Resource
    Two-dimensional polyacrylamide gel electrophoresis, with immobilized pH gradients in the first dimension, of barley seed proteins: Discrimination of cultivars with different malting grades (1992)
    Weinheim : Wiley-Blackwell
    Electrophoresis 13 (1992), S. 192-203 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The suitability of high-resolution two-dimensional gel electrophoresis for barley cultivar discrimination and for classification with respect to their malting properties was studied. Seed proteins of 14 barley cultivars with different malting qualities were extracted with urea/dithiothreitol/Nonidet P-40 buffer and subjected to two-dimensional gel electrophoresis with immobilized pH gradients in the first dimension (IPG-DALT). The results of IPG-DALT were compared to the protein patterns obtained by a standard technique, sodium dodecyl sulfate polyacrylamide gel electrophoresis of hordeins. Sodium dodecyl sulfate-gel electrophoresis yielded seven different “B” and four different “C” hordein patterns; “A” and “D” hordein patterns were uniform in all cultivars tested. Four cultivars could be distinguished unequivocally, the others were classified into three groups containing between two and five cultivars. In contrast to these findings, IPG-DALT yielded three different “A”, eight different “B”, four different “C” and two different “D” hordein patterns. When the “A”, “B”, “C” and “D” hordein patterns were combined, ten cultivars exhibited unique hordein patterns whereas the remaining ones were classified into two groups containing two cultivars each. Moreover, when albumin and globulin proteins were used for evaluation in addition to the hordeins, all cultivars could be discriminated by IPG-DALT. IPG-DALT, performed on small-scale and/or ready-made gels, proved to be an ideal complementary system to one-dimensional electrophoretic methods for routine seed testing purposes because of its speed, reliability, and simplicity. IPG-DALT was also applied to study the relationship between the different polypeptide patterns and the malting quality. Although cultivars with identical one-dimensional protein patterns but different malting quality could be successfully differentiated by IPG-DALT, a direct correlation between specific protein spots or protein patterns to the malting quality was not found within the cultivars tested.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150130141
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  • 23
    Electronic Resource
    Electronic Resource
    Two-dimensional polyacrylamide gel electrophoresis with immobilized pH gradients in the first dimensin (IPG-Dalt): The state of the art and the controversy of vertical versus horizontal systems (1995)
    Weinheim : Wiley-Blackwell
    Electrophoresis 16 (1995), S. 1079-1086 
    Details
    ISSN: 0173-0835
    Keywords: Two-dimensional polyacrylamide gel electrophoresis ; Immobilized pH gradients ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: After having established the basic protocol of two-dimensional electrophoresis with immobilized pH gradients in the first dimension (IPG-Dalt) in 1988 (A. Görg et al., Electrophoresis 1988, 9, 531-546), some critical parameters of the actual IPG-Dalt protocols as well as the results obtained with horizontal and vertical second-dimensional sodium dodecyl sulfate-electrophoresis are demonstrated and discussed.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.11501601183
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  • 24
    Electronic Resource
    Electronic Resource
    Identification and characterization of wheat grain albumin/globulin allergens (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 826-833 
    Details
    ISSN: 0173-0835
    Keywords: Allergy ; Bakers' asthma ; Immobilized pH gradient ; Amino acid sequence analysis ; Two-dimensional polyacrylamide gel electrophoresis ; Wheat ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Bakers' asthma, an immediate-type allergic response to the inhalation of cereal flours, is an important occupational disease among workers of the baking and milling industries, and the salt-soluble proteins of wheat and rye flour dust are considered the most relevant allergens. In order to identify and characterize the major IgE-binding proteins, the polypeptide composition of the albumin/globulin protein fraction obtained from different cultivars was analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and high-resolution two-dimensional polyacrylamide gel electrophoresis with immobilized pH gradients in the first dimension (IPG-Dalt), followed by immunoblotting with sera from asthmatic bakers. Relevant allergens were isolated by micropreparative IPG-Dalt and blotting onto polyvinylidenedifluoride membranes and identified by amino acid composition analysis or N-terminal amino acid sequence analysis. SDS-PAGE, IPG-Dalt, and immunoblotting demonstrated that the sera of the bakers allergic to flour contained IgE antibodies which bound to numerous albumin/globulin polypeptides in the 70, 55, 35, 26-28, and 14-18 kDa areas. More detailed investigations using IPG-Dalt revealed cultivar-specific differences in IgE-binding. It was also demonstrated that the majority of the allergens were not single polypeptide spots, but consisted of up to ten isoforms of similar molecular mass but different isoelectric points. Amino acid composition analysis and N-terminal amino acid sequence analysis, which were performed for nine allergens located in the 14-18, 26-28, and 35 kDa areas, revealed homologies to amylase/protease inhibitors, acyl-CoA oxidase and fructose-bisphosphate-aldolase from wheat, barley, maize, and rice, respectivelyPresented at the “Elektrophorese Forum “96” meeting of the German Electrophoresis Society, held at the Technical University Munich, October 23-25, 1996.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150180529
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  • 25
    Electronic Resource
    Electronic Resource
    Application of sequential extraction procedures and glycoprotein blotting for the characterization of the 2-D polypeptide patterns of barley seed proteins (1992)
    Weinheim : Wiley-Blackwell
    Electrophoresis 13 (1992), S. 770-773 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Barley (Hordeum vulgare L.) proteins were sequentially extracted from ground seeds with Tris-HCl buffer, 55% 2-propanol, 55% 2-propanol containing 1% dithiothreitol, and 6 M urea containing 2 % Nonidet P-40 and 1 % dithiothreitol. The protein composition of these solubility fractions was then analyzed by high resolution two-dimensional gel electrophoresis with immobilized pH gradient 4-9 in the first dimension, followed by silver staining and glycoprotein blotting, respectively, for a more detailed characterization of the two-dimensional polypeptide pattern of barley seed proteins.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.11501301167
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  • 26
    Electronic Resource
    Electronic Resource
    Electrophoretic characterization of wheat grain allergens from different cultivars involved in bakers' asthma (1993)
    Weinheim : Wiley-Blackwell
    Electrophoresis 14 (1993), S. 805-816 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: In order to identify and characterize the wheat grain allergens involved in bakers' asthma, proteins were sequentially extracted from whole-meal flour. The polypeptide composition of the individual solubility fractions (albumin/globulin, gliadin and glutenin) was analyzed by sodium dodecyl sulfate-gel electrophoresis (SDS-PAGE), and high-resolution two-dimensional gel electrophoresis with immobilized pH gradient 4-9 in the first dimension (IPG-Dalt). The resolved polypeptides were transferred onto an immobilizing polyvinylidene difluoride membrane and incubated with a pooled serum from four asthmatic bakers. Bound IgE was demonstrated by autoradiography using 125I-labeled anti-human IgE. Our study demonstrated that the serum of the bakers allergic to flour contained IgE antibodies which bound to numerous polypeptides of all three solubility fractions. The highest percentage of IgE binding was observed with certain albumin and/or globulin polypeptides, whereas the gliadins and glutenins exhibited considerably less allergenicity. SDS-PAGE revealed that the protein which bound the highest percentage of IgE from the sera of the allergic bakers is a 27 kDa albumin. More detailed investigations using IPG-Dalt demonstrated that this allergen is not a single polypeptide but consists of several polypeptide spots that differ in their isoelectric points. Quantitative studies using computer-assisted laser densitometry revealed that the amount of patients' IgE bound by these particular polypeptides differed considerably between the seven wheat cultivars examined, ranging from 13% to 53% of the total radioactive uptake.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.11501401126
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  • 27
    Electronic Resource
    Electronic Resource
    Two-dimensional electrophoresis of proteins in an immobilized pH 4-12 gradient (1998)
    Weinheim : Wiley-Blackwell
    Electrophoresis 19 (1998), S. 1516-1519 
    Details
    ISSN: 0173-0835
    Keywords: Alkaline proteins ; Wide immobilized pH gradient ; Mouse liver ; Ribosomal proteins ; Two-dimensional polyacrylamide gel electrophoresis ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: For checking theoretical two-dimensional (2-D) maps derived from sequenced genomes, indicating that nonnegligible amounts of proteins up to pH 12 are to be expected, a wide-range immobilized pH 4-12 gradient was generated. Depending on the extraction method of sample preparation, proteins with pIs up to pH 12 are detected in a single gel. Highly reproducible protein patterns focused to the steady state with round-shaped spots up to pH 12 are obtained with the standard protocol originally described in 1988 (Görg et al., Electrophoresis 1988, 9, 531-546).
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150190850
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