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  • 11
    Electronic Resource
    Electronic Resource
    Detection of polypeptides and amylase isoenzyme modifications related to malting quality during malting process of barley by two-dimensional electrophoresis and isoelectric focusing with immobilized pH gradients (1992)
    Weinheim : Wiley-Blackwell
    Electrophoresis 13 (1992), S. 759-770 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Two cultivars (“Alexis” and “Lenka”) of contrasting final attenuation values were malted, and the protein and amylase isoenzyme composition, as well as the change in protein and amylase isoenzyme composition during malting, was investigated by two-dimensional polyacrylamide gel electrophoresis of total proteins, and isoelectric focusing of amylase isoenzymes, respectively. Isoelectric focusing demonstrated that significant differences exist between the amylase isoenzyme patterns of the two cultivars, suggesting a correlation between the presence of certain amylase isoenzyme bands and final attenuation. This finding was confirmed by analysis of 36 barley cultivars with a wide range of quality. It was shown that all cultivars which are of low or, at best, moderate final attenuation values exhibit the amylase band “B” (isoelectric point ≍ 6.8), whereas those cultivars which are predominantly of high malting grade do not possess this “B” isoenzyme band, but exhibit the pronounced “A” isoenzyme band (isoelectric point ≍ 6.5) instead, suggesting that these isoenzymes (which we suppose to be β-amylases) can be utilized to predict the final attenuation values of unknown barley samples or new lines. However, “final attenuation” is a complex function. Preliminary results of two-dimensional gel electrophoresis indicate that other factors, such as total amount of amylases, or a 19 kDa A hordein-like polypeptide, which was degraded faster in the low malting grade cultivar “Lenka”, may also have a role in determining quality.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.11501301166
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  • 12
    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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  • 13
    Electronic Resource
    Electronic Resource
    Low fluorescence background electroblotting membrane for DNA sequencing (1992)
    Weinheim : Wiley-Blackwell
    Electrophoresis 13 (1992), S. 105-114 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: A low fluorescence background polypropylene (PP) membrane has been developed for ultimate use as an electroblotting membrane in DNA sequencing based on fluorescence detection. The DNA binding capacity of this membrane is improved by a surface modification using radio frequency plasma discharge (RFPD) in ammonia gas. The RFPD operational parameters are evaluated both in terms of membrane nitrogen content and in terms of the product's capacity for binding radioisotope-labeled DNA fragments. The surface morphologies of the derivatized membranes are examined by scanning electron microscopy; their mechanical and electrical properties, which are important for the subsequent sequencing procedures, are likewise established. Due to the goal of developing a membrane suitable for multiplex processing, in which the electroblotted DNA must withstand dozens of hybridization/stripping cycles, special attention is given the covalent attachment of DNA to the membrane. The modified PP membrane is evaluated in a multiplex sequencing application using radioisotope-labeled DNA probes, and found to yield somewhat better binding of a given amount of electroblotted DNA than the commonly used GeneScreen membrane. A tenfold repetition of the probing indicates little loss of signal; the membrane-bound DNA is stable upon storage and shows no detectable loss in probing efficiency after one month.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150130124
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  • 14
    Electronic Resource
    Electronic Resource
    A comparison of resolution of DNA fragments between agarose gel and capillary zone electrophoresis in agarose solutions (1995)
    Weinheim : Wiley-Blackwell
    Electrophoresis 16 (1995), S. 1345-1353 
    Details
    ISSN: 0173-0835
    Keywords: Resolution ; DNA ; Capillary zone electrophoresis ; Gel electrophoresis ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The resolving power of capillary zone electrophoresis (CZE) is compared to that of gel electrophoresis (GE) under similar conditions (agarose, similar length of DNA fragments, identical buffer) but with differences in temperature and field strength. The comparison is based on the time required to reach a desired degree of resolution by each of the two methods. A resolution parameter is developed which is equally applicable to CZE, with relatively diffuse initial conditions in the absence of stacking and measurements expressed in terms of time, and to GE, in which measurements are expressed in terms of spatial parameters. The resolution time in CZE using agarose solutions at 40°C was found to be greater by at least one order of magnitude than that in GE using agarose gels. Thus, the increased migration velocity due to high field strength in CZE substantially outweights the lower dispersion in GE.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.11501601222
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  • 15
    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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  • 16
    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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  • 17
    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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  • 18
    Electronic Resource
    Electronic Resource
    Some properties of a measure of resolution in gel electrophoresis and capillary zone electrophoresis (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 2008-2011 
    Details
    ISSN: 0173-0835
    Keywords: Gaussian peaks ; Capillary electrophoresis ; Gel electrophoresis ; Resolution ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The most commonly used measure of resolution for chromatographic and electrophoretic separations does not take into account the possibility of there being different amounts of each of the molecular species. A modification of a measure of resolution recently suggested by Aldroubi and Garner (BioTechniques 1992, 13, 620-624) can incorporate this effect explicitly. Their criterion for resolution is based on the time to observe a valley of specified magnitude separating two peaks. We examine how this measure depends on different physically relevant parameters that characterize the system.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150181121
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  • 19
    Electronic Resource
    Electronic Resource
    Isoelectric focusing in immobilized pH gradients with carrier ampholytes added for high-resolution phenotyping of bovine β-lactoglobulins: Characterization of a new genetic variant (1988)
    Weinheim : Wiley-Blackwell
    Electrophoresis 9 (1988), S. 609-613 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The genetic variants of bovine β-lactoglobulin (β-lg) from the “Murnau-Werdenfelser” breed were analyzed in three different isoelectric focusing (IEF) systems. While carrier ampholyte IEF with a pH gradient of 0.2 pH/cm did not resolve the new variant W from the B variant and IEF in immobilized pH gradients (IPG) with 0.1 pH/cm only partially resolved it, adequate separation was achieved with IPG-IEF in a pH 5.25-pH 5.7 gradient, in presence of 0.8 % w/v carrier ampholytes, both over a 10 and 17 cm separation distance. Apparent isoelectric points (pI's) and genetic frequencies (f) were as follows: β-lg A, pI = 5.370,f = 0.364; β-lg B, pI = 5.485,f = 0.480; β-lg W, pI = 5.492,f = 0.076; and β-lg D, pI = 5.610,f = 0.080. The small difference of Δ pI = 0.007 between β-lg B and β-lg W respectively, seems to originate from a “silent” substitution of neutral amino acid residues as compared to the larger Δ pI's of the other genetic variants of β-lg, which result from substitution of charged amino acids.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150090925
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  • 20
    Electronic Resource
    Electronic Resource
    Studies on 16 kDa selenium-containing proteins enriched by means of preparative electrophoresis (1993)
    Weinheim : Wiley-Blackwell
    Electrophoresis 14 (1993), S. 108-111 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: By in vivo labeling with [75Se]selenite and separation of the proteins in the tissue homogenates by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), several selenium-containing proteins or protein subunits were detected in rat tissues (liver, lung, spleen and prostate). Their distribution among the cell components was investigated after fractionation by means of differential centrifugation. The selenium-containing proteins in the 16 kDa range were found to be mainly membrane-bound. By two-dimensional electrophoresis they were resolved into three labeled spots, two with the same relative molecular mass and pI values of about 4.8 and 5.0 and the third with a slightly lower molecular mass and a pI of 4.8. For further investigation they were concentrated and separeted from the other labeled compounds by SDS-PAGE using preparative flow-through electrophoresis.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150140119
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