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  • 1
    Electronic Resource
    Electronic Resource
    Microbially produced rhamnolipid as a source of rhamnose (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 33 (1989), S. 365-368 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260330316
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  • 2
    Electronic Resource
    Electronic Resource
    Conformational Behavior of C-Glycosyl Analogues of Sialyl-α-(2→3)-Galactose (2000)
    Weinheim : Wiley-Blackwell
    Liebigs Annalen 2000 (2000), S. 1805-1813 
    Details
    ISSN: 1434-193X
    Keywords: C-Glycosides ; Conformation analysis ; Molecular dynamics ; Selectins ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: ---The conformational behavior of the C-glycosyl analogue of sialyl-α-(2→3)-galactose, synthesized as a glycosidase inhibitor, has been studied using a combination of NMR spectroscopy (J and NOE data) and molecular dynamics calculations. The obtained results show that the population distribution of conformers with respect to the orientation about the pseudo-glycosidic linkages is mainly controlled by steric interactions. This is in contrast to findings made for O-glycosides. In these natural compounds, the conformational behavior about the glycosidic linkage Φ is mainly governed by the exo-anomeric effect.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Randomness in the heparin polymer: Computer simulations of alternative action patterns of heparin lyase (1990)
    New York : Wiley-Blackwell
    Biopolymers 30 (1990), S. 733-741 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Heparin is a mixture of linear polysaccharides of undetermined sequence. Both biosynthetic data and computer simulation studies have established that each heparin polymer chain is comprised of oligosaccharides of defined sequence, representing ordered domains. One such ordered domain is a pentasaccharide corresponding to heparin's antithrombin III binding site. Previous computer simulation studies, performed under the assumption that heparin lyase (heparinase, EC 4.2.2.7), has a random endolytic action pattern, suggested that certain of these ordered oligosaccharide domains may themselves be nonrandomly arranged in the heparin polymer. The present, work presents computer simulations of alternative action patterns for heparin lyase while assuming a random distribution of these oligosaccharide units within the heparin polymer. We consider action patterns that are determined solely by the primary structure of the substrate molecules. Results of the simulations are compared to (1) the experimental measurements of product chains formed throughout the reaction and (2) the change in weight average molecular weight Mw as a function of reaction completion as determined by absorbance at 232 nm.From the simulation of 60 action patterns for heparin lyase, we infer that one of the following statements concerning heparin and heparin lyase is true: (1) Heparin is a random arrangement of a small number of structurally defined oligosaccharide units. Heparin lyase changes its action pattern during the depolymerization of heparin (perhaps influenced by the secondary structure of substrate). (2) Heparin contains clusters of oligosaccharide sequences that are present in low concentrations (overall) in the polymer. Heparin lyase has a specificity for cleaving glycosidic linkages either exolytically at the nonreducing terminus of a chain or (endolytically) at the reducing side of these rare oligosaccharide sequences.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360300708
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  • 4
    Electronic Resource
    Electronic Resource
    Isolation and recovery of acidic oligosaccharides from polyacrylamide gels by semi-dry electrotransfer (1990)
    Weinheim : Wiley-Blackwell
    Electrophoresis 11 (1990), S. 23-28 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Acidic oligosaccharides derived from glycosaminoglycan heparin were separated by polyacrylamide gradient gel electrophoresis (PAGE). The gel could be visualized using Alcian Blue dye to give a pattern of highly resolved, well defined bands. The particular banding pattern obtained was the result of a heparinase catalyzed depolymerization which afforded oligosaccharide products that differed in size by one disaccharide unit. The separated oligosaccharides could be recovered prior to staining by electroelution onto a positively charged nylon membrane by a semi-dry transfer procedure. Subsequent elution and quantitative recovery of individual oligosaccharides from the membrane was achieved. By using multiple membrane layers a second separation dimension was obtained, resulting in increased oligosaccharide purity proportional to transfer depth. Preparative gradient polyacrylamide gel electrophoresis followed by semi-dry electro-transfer and recovery represents a novel method for the preparation of homogeneous acidic oligosaccharides.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150110106
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  • 5
    Electronic Resource
    Electronic Resource
    Capillary zone electrophoresis for the quantitation of oligosaccharides formed through the action of chitinase (1991)
    Weinheim : Wiley-Blackwell
    Electrophoresis 12 (1991), S. 636-640 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Capillary zone electrophoresis with fluorescence detection was used to analyze the products formed by chitinase acting on N-acetylchitooligosaccharide-fluorescent conjugates. Six oligosaccharides of the structure [N-acetylglucosamine(1→4)]n (where n = 1-6) were conjugated to 7-amino-1,3-naphthalene disulfonic acid by reductive amination. Each oligosaccharide-fluorescent conjugate was purified by preparative gradient polyacrylamide gel electrophoresis, semi-dry electrotransfer to a positively-charged nylon membrane and recovered by washing the membrane with salt solution. The products formed by treating each oligosaccharide-fluorescent conjugate with chitinase were analyzed by capillary zone electrophoresis. The chitinase treatment hexasaccharide-fluorescent conjugate was also examined kinetically to study the action pattern of this enzyme.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150120907
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  • 6
    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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  • 7
    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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  • 8
    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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  • 9
    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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