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  • 1
    Electronic Resource
    Electronic Resource
    Affinity capillary electrophoresis employing immobilized glycosaminoglycan to resolve heparin-binding peptides (1998)
    Weinheim : Wiley-Blackwell
    Electrophoresis 19 (1998), S. 437-441 
    Details
    ISSN: 0173-0835
    Keywords: Glycosaminoglycan ; Affinity ; Capillary electrophoresis ; Heparin-binding peptides ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: A new capillary electrophoresis technique has been developed for the affinity resolution of synthetic heparin-binding peptides using an immobilized glycosaminoglycan. Heparin and heparan sulfate were immobilized onto fused silica capillaries using biotin-neutravidin conjugation. These capillaries exhibited markedly reduced electroosmotic flow and were able to distinguish peptides based on the heparin binding domain of acidic fibroblast growth factor (residues 125-144, GLKKNGSCKRGPRTHYGQKA) that differed only in the stereochemistry of the proline amino acid residue. The peptide based on the native sequence was retarded compared to the peptide having unnatural stereochemistry, consistent with its stronger interaction for immobilized glycosaminoglycan. Improved resolution is also obtained for additional arginine and lysine containing heparin-binding peptides.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150190313
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  • 2
    Electronic Resource
    Electronic Resource
    Detection of glycosaminoglycans as a copper (II) complex in capillary electrophoresis (1996)
    Weinheim : Wiley-Blackwell
    Electrophoresis 17 (1996), S. 341-346 
    Details
    ISSN: 0173-0835
    Keywords: Glycosaminoglycans ; Capillary electrophoresis ; Copper (II) sulfate ; Oligosaccharides ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Glycosaminoglycans including heparin, heparan sulfate, chondroitin sulfate, dermatan sulfate and hyaluronic acid were analyzed by reversed polarity capillary electrophoresis. Detection was achieved at 240 nm based on the formation of a copper (II) complex in copper sulfate solution at low pH. Glycosaminoglycans having a high ratio of iduronic acid to glucuronic acid, as well as ones having lower molecular weight, gave the highest detection sensitivity using this method. Detection of the copper (II)-heparin complex is extremely sensitive, permitting the analysis of as little as 10-9 g. This method was also successfully applied to the analysis of heparin oligosaccharides that lacked a chromophore prepared from heparin using controlled, low pH nitrous acid depolymerization.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150170209
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  • 3
    Electronic Resource
    Electronic Resource
    Isolation and characterization of β-cyclodextrin sulfates by preparative gradient polyacrylamide gel electrophoresis, capillary electrophoresis and electrospray ionization - mass spectrometry (1998)
    Weinheim : Wiley-Blackwell
    Electrophoresis 19 (1998), S. 2677-2681 
    Details
    ISSN: 0173-0835
    Keywords: Cyclodextrin sulfate ; Glycosaminoglycan ; Polyacrylamide gel electrophoresis ; Capillary electrophoresis ; Electrospray ionization ; Mass spectrometry ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: A β-cyclodextrin sulfate mixture has been fractionated using discontinuous gradient polyacrylamide gel electrophoresis. Semidry electrotransfer of the sample onto a positively charged nylon membrane and visualization of a portion of this membrane with Alcian blue stain showed multiple bands. The bands were cut from the remaining portion of the membrane and after washing with 8 M urea, the β-cyclodextrin sulfate fractions were eluted with 2 M sodium chloride and dialyzed. Analysis of each fraction using high resolution analytical gradient polyacrylamide gel electrophoresis as well as capillary electrophoresis, using indirect detection, showed some of the fractions to be pure while others were mixtures. Each β-cyclodextrin sulfate fraction was complexed with a basic synthetic peptide and analyzed by electrospray ionization mass spectrometry to define the mass of the components in each mixture and thereby to determine the purity of each sample.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150191517
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  • 4
    Electronic Resource
    Electronic Resource
    Capillary affinity chromatography and affinity capillary electrophoresis of heparin binding proteins (1998)
    Weinheim : Wiley-Blackwell
    Electrophoresis 19 (1998), S. 2650-2653 
    Details
    ISSN: 0173-0835
    Keywords: Capillary affinity chromatography ; Affinity chromatography ; Capillary electrophoresis ; Heparin ; Protein ; Interaction ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: A new approach for separation, capillary affinity chromatography, is introduced for studying the interaction of heparin with antithrombin III and secretory leukocyte proteinase inhibitor. Heparin is covalently immobilized on the surface of an etched capillary through a silane spacer. The proteins are injected into the heparinized capillary, bound to the heparin, washed with buffer, eluted with sodium chloride in the same buffer using a pressure injection mode and eluting protein detected by absorbance. The resulting affinity separation is similar to that obtained from traditional affinity chromatography. The quantity of loaded protein in capillary affinity chromatography is at the nanogram level, offering an improvement over the milligram levels required for standard affinity chromatographic methods.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150191514
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