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  • 1
    Electronic Resource
    Electronic Resource
    High resolution two-dimensional electrophoresis of hair proteins without prior S-carboxymethylation (1986)
    Weinheim : Wiley-Blackwell
    Electrophoresis 7 (1986), S. 524-526 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Hair proteins have been successfully analysed by high resolution two-dimensional electrophoresis by avoiding S-carboxymethylation which has previously dictated the use of alternative two-dimensional procedures. The high and low-sulfur proteins are simultaneously resolved within the pI range 3-9 and their electrophoretically determined Mr values are consistent with molecular weights obtained by physical methods.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150071108
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  • 2
    Electronic Resource
    Electronic Resource
    The effect of narrow pH range ampholytes upon resolution and protein detection methods following two-dimensional electrophoresis (1986)
    Weinheim : Wiley-Blackwell
    Electrophoresis 7 (1986), S. 567-569 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Ampholine pH 4-6 and Pharmalyte pH 4.2-4.9, 4.5-5.4 or 5-6 have been used to improve the resolution of the simplified technique of high resolution two-dimensional electrophoresis. All give excellent resolution but Pharmalyte interferes with protein detection methods to an extent which increases with the pH range of the mixture. The effect is characterised by a progressive increase in the intensity and area of background stain associated with the anode and cathode regions of the two-dimensional gels. It is minimal following Serva Blue R (Coomassie Blue) staining but severe following silver staining.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150071206
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  • 3
    Electronic Resource
    Electronic Resource
    An evaluation of two-dimensional electrophoresis for detection of human serum proteins in acute myocardial infarction (1988)
    Weinheim : Wiley-Blackwell
    Electrophoresis 9 (1988), S. 672-675 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: High resolution two-dimensional electrophoresis indicates that serum proteins previously only detected in patients with acute myocardial infarction (AMI) (Gomo et al., Electrophoresis 1983, 4, 298-302) are also present in the serum protein patterns of other patients (AMI negative or demonstrating acute phase response) and are faintly detected even in controls. Thus, these proteins are not specific to AMI and are probably acute phase reactants. However, they do demonstrate a characteristic time course response in sequential samples from AMI patients.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150091009
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  • 4
    Electronic Resource
    Electronic Resource
    Sodium dodecyl sulfate-polyacrylamide gel electrophoresis without a stacking gel: Use for high sample throughput (1989)
    Weinheim : Wiley-Blackwell
    Electrophoresis 10 (1989), S. 63-65 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Sodium dodecyl sulfate-polyacrylamide gel electrophoresis without a stacking gel minimizes lateral spreading of protein when samples are applied in agarose wells and allows high sample throughput (6 samples/cm gel width). The method is simple and convenient to use and gives comparable resolution to the standard method with 4-20% or 6-30% polyacrylamide gradient gels. Best results are obtained when the upper zone of the separating gel is of low polyacrylamide concentration. This indicates a need for the molten agarose to penetrate and anneal with the separating gel.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150100115
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  • 5
    Electronic Resource
    Electronic Resource
    Two-Dimensional electrophoresis of human serum proteins following acute myocardial infarction (1989)
    Weinheim : Wiley-Blackwell
    Electrophoresis 10 (1989), S. 584-588 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Serum proteins associated with acute myocardial infarction (AMI) have been monitored by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and high resolution two-dimensional electrophoresis (2-DE) under nonreducing conditions. Proteins a, b, c (Mr 13 000; pI 6.2, 6.7 and 7.5, respectively) and e (Mr 27 000; pI 5.2) appear simultaneously ∼ 30 h after infarction, reach maximum intensity after 48 h and progressively decline thereafter. Protein d (Mr 15 000; pI 7-8.5; identified as hemoglobin) sometimes appears within 18 h of infarction. Proteins a-c are not detected in the 2-DE patterns of healthy myocardium, infarcted myocardium, pectoral muscle or tongue, but e is present in all and tentatively identified as myosin light chain. Other myocardial proteins which are either reduced in amount following infarction or more specifically associated with myocardium than pectoral muscle are not detected in the serum of AMI patients. Analysis of unconcentrated urine by SDS-PAGE and silver staining does not reveal proteins specific to AMI.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150100809
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  • 6
    Electronic Resource
    Electronic Resource
    Recovery of protein by Coomassie Brilliant Blue precipitation prior to electrophoresis (1992)
    Weinheim : Wiley-Blackwell
    Electrophoresis 13 (1992), S. 887-888 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The interaction of protein with Coomassie Brilliant Blue G-250 results in formation of an insoluble protein-dye complex which can be recovered by centrifugation and redissolved for electrophoretic analysis. The precipitated protein can be washed in acetone to remove excess dye in order to enhance resolution. The residual dye becomes dissociated from the proteins on electrophoresis and can be exploited as a “dye front”. The method allows simultaneous protein assay and recovery of microgram amounts of protein from dilute solution and could be widely applied for conserving, concentrating and desalting minute amounts of valuable sample prior to electrophoretic analysis.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.11501301195
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  • 7
    Electronic Resource
    Electronic Resource
    Protein concentration by precipitation with pyrogallol red prior to electrophoresis (1995)
    Weinheim : Wiley-Blackwell
    Electrophoresis 16 (1995), S. 28-31 
    Details
    ISSN: 0173-0835
    Keywords: Protein concentration ; Pyrogallol red ; Urinary proteins ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The pyrogallol red protein assay (Clinical Chemistry 1986, 32, 1551-1554) is based upon formation of a blue protein-dye complex in the presence of molybdate under acidic conditions. However, centrifugation of the assay mixture results in loss of color yield and precipitation of the protein-dye complex which can be recovered and resolubilized to achieve protein concentration prior to sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The method has been evaluated relative to trichloroacetic acid (TCA) precipitation for recovery and electrophoresis of commercial protein and peptide molecular weight markers. Precipitation with pyrogallol red-molybdate (PRM) gives better and more uniform recovery of both proteins and peptides as compared to TCA. The lower limit of PRM precipitation is similar to TCA and corresponds to 1 μg protein per mL assay mixture. This is equivalent to 100 μL of 10 μg/mL protein using the standard protein assay or 1 μg/mL protein using a modified assay incorporating a fivefold concentrate of the dye reagent. Application of the method is demonstrated by concentration of urinary proteins. The method is simple and economic and useful for conserving trace amounts of precious sample as it allows recovery of protein for electrophoresis following protein assay.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150160107
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  • 8
    Electronic Resource
    Electronic Resource
    High resolution two-dimensional electrophoresis of the proteins and macromolecular constituents of beer and wine (1987)
    Weinheim : Wiley-Blackwell
    Electrophoresis 8 (1987), S. 493-495 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The proteins/macromolecular constituents of unconcentrated/unfractionated beer and wine (50-75 μL) have been analyzed by high resolution two-dimensional electrophoresis and silver staining. The beer patterns are dominated by up to four horizontal strings of spots of Mr 34 000-43 000 and pI 5.0-7.0 which have been tentatively identified as proteins previously isolated in association with foam and haze formation. Reproducible qualitative and quantitative differences were detected in different commercial beers. Distinctive patterns were also obtained with the wines.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150081008
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  • 9
    Electronic Resource
    Electronic Resource
    High resolution two-dimensional electrophoresis and sodium dodecyl sulphate-polyacrylamide gel electrophoresis of cheese proteins after rapid solubilisation (1988)
    Weinheim : Wiley-Blackwell
    Electrophoresis 9 (1988), S. 143-147 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The proteins of cheese are rapidly solubilised by heating to 95 °C in buffered 2 % sodium dodecyl sulfate, 5 % 2-mercaptoethanol. Electrophoretic analysis of the solubilised proteins by either one-dimensional sodium dodecyl sulphate-polyacrylamide gel electrophoresis or high resolution two-dimensional electrophoresis yields reproducible patterns characteristic of an individual cheese and its extent of ripening. The patterns reveal (i) the residual amounts of milk casein and whey proteins, and (ii) the appearance of casein degradation products, including pink-violet components as detected by Coomassie Blue staining.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150090308
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  • 10
    Electronic Resource
    Electronic Resource
    A comparison of two-dimensional gel electrophoresis methods for analysis of rat serum proteins following dimethylformamide exposure (1985)
    Weinheim : Wiley-Blackwell
    Electrophoresis 6 (1985), S. 392-398 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Four two-dimensional electrophoresis methods, each incorporating different protein denaturing/dissociating conditions, have been used to detect changes in rat serum proteins following exposure to dimethylformamide. The methods were evaluated on the basis of (i) their ability to detect changes, (ii) the resolution achieved and (iii) the response of resolution to the use of narrow Ampholine pH ranges in the first dimensional isoelectric focusing gels. All methods reveal minor but reproducible protein changes in response to dimethylformamide. However, high resolution two-dimensional electrophoresis of the completely dissociated polypeptides reveals most changes and the resolution of this method is most improved by the use of Ampholines of narrow pH range. In general, the number of serum components detected and the resolution achieved is related to the severity of the protein denaturing/dissociating conditions employed. The significance of this observation in relation to others factors likely to influence the choice of two-dimensional method is discussed.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150060808
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