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  • 11
    Electronic Resource
    Electronic Resource
    Scientists in Conference. Volker Neuhoff, VCH Verlagsgesellschaft, Weinheim 1987, 223 pages, DM 58,-/US$ 38.50, ISBN 3-527-26579-1 (1988)
    Weinheim : Wiley-Blackwell
    Electrophoresis 9 (1988), S. 291-291 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150090609
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  • 12
    Electronic Resource
    Electronic Resource
    The application of direct tissue isoelectric focusing to the study of human skeletal muscle (1981)
    Weinheim : Wiley-Blackwell
    Electrophoresis 2 (1981), S. 251-258 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: A method of direct tissue isoelectric focusing (DTIF) in agarose of human skeletal muscle is described. This particular method was developed to utilize the small amounts of tissue obtained by needle muscle biopsies performed for diagnostic purposes. 20 μm thick cryostat sections were adhered to the hydrophilic surfaces of small GelBond rectangles. These were then applied directly to the surface of the gels. A charge-balanced purified agarose was used to make the gels, which contained Triton X-100 to enhance protein solubilization. Stabilization of the pH gradient was attempted by employing a 3% w/v ampholyte which was a blend of 0.85% w/v pH 8-10.4 and 2.15 % w/v pH 3-10 Pharmalyte, by using anolyte regulation with 0.1 M aspartic acid and by focusing the gels under a CO2-extracted nitrogen atmosphere. Equilibrium of proteins stained by Coomassie Brilliant Blue R-250 was apparent as monitored by comigration of sections from both anode and cathode. With the exception of the cathode end, excellent resolution and reproducibility was achieved. Better cathode resolution was noted with non-equilibirium conditions. Preliminary zymograms of lactic dehydrogenase (LDH), using a tetrazolium technique, have shown consistent patterns of multiple isoenzymes, the basic components of which were best seen using non-equlibirium conditions.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150020410
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  • 13
    Electronic Resource
    Electronic Resource
    A comparative study of protein synthesis by keratinocytes and fibroblasts in vitro using two-dimensional gel electrophoresis and dual isotope autoradiography (1988)
    Weinheim : Wiley-Blackwell
    Electrophoresis 9 (1988), S. 227-231 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: A procedure is described for the detection of keratinocyte specific proteins. Fibroblasts and keratinocytes were isolated from human skin and radiolabelled in vitro. Samples were separated by two-dimensional polyacrylamide gel electrophoresis to compare the proteins synthesised by the different types of cultured skin cells. Dual label autoradiography of samples radiolabelled with [35S]methionine and [75Se]selenomethionine was used to identify keratinocyte specific proteins. We report 45 keratinocyte-specific components and identify some of these proteins. The differential expression of these proteins and their relevance to epidermal differentiation are discussed.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150090507
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  • 14
    Electronic Resource
    Electronic Resource
    Analysis of skin fibroblast proteins in Duchenne muscular dystrophy: 1. Sodium dodecyl sulphate polyacrylamide gel electrophoresis (1982)
    Weinheim : Wiley-Blackwell
    Electrophoresis 3 (1982), S. 177-185 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Protein profiles of skin fibroblasts from patients with Duchenne muscular dystrophy (DMD) and normal individuals have been compared using polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate (SDS) combined with various detection systems. Protein patterns of normal and DMD fibroblasts obtained usin 10 % polyacrylamide gels showed no qualitative or quantitative differences. The use of acrylamide gels results in increased resolution. No qualitative or quantitative differences were observed using Coomassie Brilliant Blue R-250 staining. However, Coomassie Brilliant Blue lacks the sensitivity to detect many minor components. Therefore a silver staining procedure was used, which resulted in greatly increased detection sensitivity. Background staining did not increase with gel concentration, but stain development proceeded more slowly at higher acrylamide concentrations. No qualitative differences were observed between normal and DMD profiles. Fibroblasts radiolabelled with [35S]-methionine were analysed using gradient gels. No qualitative differences between DMD and normal patterns were observed by autoradiography of dried gels. However, quantitative analysis of slicing of gel rods revealed differences between normal and DMD fibroblasts. Two methods of statistics were used to analyse this data, firstly a method that accounts for inter-experimental variation (termed “batch statistics”) and secondly the standard t-test. Regions of 73 000 to 68 000 and 48 000 molecular weight were decreased in DMD samples and this finding was significant by both methods of statistical analysis. Regions of 175 000 and 53 000 molecular weight were significantly elevated in DMD preparations only by t-test, whereas a regions of 32 × 103 molecular weight was only significantly elevated when tested by batch statistics.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150030402
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  • 15
    Electronic Resource
    Electronic Resource
    Editorial (1990)
    Weinheim : Wiley-Blackwell
    Electrophoresis 11 (1990), S. 353-354 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150110419
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  • 16
    Electronic Resource
    Electronic Resource
    Evaluation of membranes used for electroblotting of proteins for direct automated microsequencing (1991)
    Weinheim : Wiley-Blackwell
    Electrophoresis 12 (1991), S. 342-348 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Protein purification and characterisation have been age-old problems for the biochemist. A new era has arisen with the advent of one- and two-dimensional gel electrophoresis and high sensitivity automated protein microsequencing. These two tools along with electroblotting have made it possible to separate and analyse complex protein mixtures. We studied six different membranes compatible with Edman degradation chemistry to determine their efficiencies at binding proteins electroblotted from one-dimensional sodium dodecyl sulphate-polyacrylamide gel electrophoresis. Their overall blotting-sequencing properties were also evaluated. We found that the polyvinylidene difluoride-based membranes out-performed the glass-based and polypropylene-based membranes under our selec ted experimental conditions. The problems associated with electroblotting and microsequencing are discussed.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150120505
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  • 17
    Electronic Resource
    Electronic Resource
    Editorial (1991)
    Weinheim : Wiley-Blackwell
    Electrophoresis 12 (1991), S. 459-460 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150120702
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  • 18
    Electronic Resource
    Electronic Resource
    A study of protein synthesis in cells cultured from involved psoriatic skin (1991)
    Weinheim : Wiley-Blackwell
    Electrophoresis 12 (1991), S. 579-584 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Using histochemical techniques an abnormal programme of epidermal differentiation has been well documented in psoriasis. In order to characterise further the biochemistry of this process we have cultured dermal fibroblasts and epidermal keratinocytes from involved psoriatic skin. This has facilitated metabolic radiolabelling of skin cells and analysis of protein synthesis by two-dimensional polyacrylamide gel electrophoresis. The expression of keratin and differentiation markers was identical to that of normal keratinocytes, suggesting that psoriatic epidermal differentiation is not truncated in vitro as has been postulated to be the case in vivo. Low molecular mass components (5-8.5 kDa), previously shown to be upregulated in suprabasal keratinocytes, were detected in epidermal fractions from psoriatic skin enriched for basal cells. Of especial interest was a component of 26 kDa, pI 5.9, which was highly upregulated in psoriatic as compared to normal cultured keratinocytes and was not detected in fibroblasts. These findings are in accord with a qualitatively abnormal pattern of differentiation for keratinocytes in the involved psoriatic epidermis.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150120718
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  • 19
    Electronic Resource
    Electronic Resource
    Positional reproducibility of protein spots in two-dimensional polyacrylamide gel electrophoresis using immobilised pH gradient isoelectric focusing in the first dimension: An interlaboratory comparison (1994)
    Weinheim : Wiley-Blackwell
    Electrophoresis 15 (1994), S. 1205-1211 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: An intra- and interlaboratory comparison of positional reproducibility of protein spots in two-dimensional electrophoresis using immobilised pH gradients (IPG) in the first dimension (IPG-DALT) was made. Aliquots of two different samples, human cardiac and barley leaf proteins, were separated in two different laboratories (London and Munich), using 180 mm long IPG gel strips, pH 4-8, for the first dimension and homogeneous SDS-PAGE gels (12% T) for the second dimension. Subsets of 340 (cardiac) and 200 (barley) well-resolved spots distributed across the 2-D gel patterns were selected for computer analysis (PDQUEST) of positional reproducibility. The IPG-dimension was highly reproducible in each laboratory, with a mean standard deviation of about 1 mm for both types of sample. Interlaboratory comparisons revealed identical results for barley with a mean standard deviation along the x-axis of about 1 mm, whereas the cardiac matchset showed slightly more variability (mean standard deviation ∼ 1.5 mm). Nevertheless, IPG-DALT provides significantly improved reproducibility of spot positions compared to conventional isoelectric focusing with synthetic carrier ampholytes.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.11501501182
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  • 20
    Electronic Resource
    Electronic Resource
    From experimental data analysis and modeling to clinical applications (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. I 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150181502
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