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  • 1
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Electrophoresis 7 (1986), S. 221-226 
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: A compact device, capable of being clipped onto the end of a 3 mm thick analytical polyacrylamide slab gel, has been developed for the collection of resolved protein zones as they elute from the end of the gel. Its unique feature is that eluted proteins were collected between two polyacrylamide-embedded paper membranes and removed either by continuous or intermittent buffer elution. Because of this direct coupling to large gels identical to those used for analytical electrophoresis, protein zones were obtained with high resolution. The method was applicable to non-denaturing cathodic and anodic electrophoresis, as well as sodium dodecyl sulfate electrophoresis. Medium-scale quantities (up to 10 mg/cm2 cross-sectional area) of protein were fractionated in as little as 4 h with high recoveries.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Electrophoresis 15 (1994), S. 968-971 
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: New equipment (the “Gradiflow TM”) has been designed and constructed to provide efficient large-scale preparative fractionation of macromolecules, based on charge and/or size differences, as well as the concentration of macromolecules and electrodialysis. Examples of its capability are the separation of a mixture of haemoglobin (50 mg) from bovine serum albumin (50 mg) within 15 min (based on charge differences at pH 6.8), the purification of phycoerythrin from a crude extract on the basis of size, and the fractionation of serum proteins into two discrete size classes.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Electrophoresis 17 (1996), S. 771-775 
    ISSN: 0173-0835
    Keywords: Preparative electrophoresis ; Large-scale electrophoresis ; Protein purification ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The Gradiflow is a preparative electrophoresis apparatus, allowing fractionation based on a combination of size and charge of proteins in their native (unreduced) form. The prepative fractionation of two proteins of similar size and isoelectric point is demonstrated using the Gradiflow. A separation membrance of appropriate pore size was chosen and then fractionation was “fine tuned” by selecting an appropriate buffer pH to accentuate charge differences between the proteins of interest. Complete separation of mg quantities of bovine serum albumin and ovalbumin was achieved within 40 minPresented at the Second Annual Meeting of the Australian Electrophoresis Society, Sydney, April 29-30, 1995..
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Electrophoresis 17 (1996), S. 224-226 
    ISSN: 0173-0835
    Keywords: Preparative affinity electrophoresis ; Gradiflow ; Dextran blue ; Serum proteins ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Using the patented Gradiflow system in conjunction with newly developed affinity membranes, the suitability of an electrokinetic technique for affinity fractionation was investigated. Blue dextran incorporated into an affinity membrane was used to deplete a solution of horse serum of albumin, with the result that a majority of serum proteins were enriched tenfold relative to albumin. The technique, when fully developed, would offer some advantages over affinity chromatography, since to a degree it is possible to control which components of the sample are presented to the affinity matrix. Furthermore, the technique would extend the capabilities of the already multifunctional Gradiflow system.
    Additional Material: 3 Ill.
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  • 5
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Electrophoresis 16 (1995), S. 98-100 
    ISSN: 0173-0835
    Keywords: Preparative electrophoresis ; Membranes ; Serum albumin ; Reflux electrophoresis ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: As part of the method for large-scale preparative electrophoresis across membranes of controlled porosity, we show that successive amounts of the leading component of a mixture migrating across a thin membrane can be collected by ‘reflux electrophoresis’. This consists of a series of cycles, in each of which the forward phase is stopped before the trailing components can emerge, the leading fraction is collected and the membrane cleared by reversing the current before commencing the next cycle. The reflux principle is demonstrated by separations based on size or on charge differences of protein molecules.
    Additional Material: 3 Ill.
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  • 6
    Publication Date: 1983-02-01
    Print ISSN: 0003-2697
    Electronic ISSN: 1096-0309
    Topics: Biology , Chemistry and Pharmacology
    Published by Elsevier
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