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  • 1
    Electronic Resource
    Electronic Resource
    Structural homology of spinach acyl carrier protein and Escherichia coli acyl carrier protein based on NMR data (1997)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 27 (1997), S. 131-143 
    Details
    ISSN: 0887-3585
    Keywords: protein structure ; protein dynamics ; molecular mechanics ; NOE ; NMR ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Acyl carrier proteins (ACPs) from spinach and from Escherichia coli have been used to demonstrate the utility of proton NMR for comparison of homologous structures. The structure of E. coli ACP had been previously determined and modeled as a rapid equilibrium among multiple conformational forms (Kim and Prestegard, Biochemistry 28:8792-8797, 1989). Spinach ACP showed two slowly exchanging forms and could be manipulated into one form for structural study. Here we compare this single form to postulated multiple forms of E. coli ACP using the limited amount of NOE data available for the spinach protein. A number of long-range NOE contacts were present between homologous residues in both spinach and E. coli ACP, suggesting tertiary structural homology. To allow a more definitive structural comparison, a method was developed to use spinach ACP NOE constraints to search for regions of structural divergence from two postulated forms of E. coli ACP. The homologous regions of the two protein sequences were aligned, additional distance constraints were extracted from the E. coli structure, and these were mapped onto the spinach sequence. These distance constraints were combined with experimental NOE constraints and a distance geometry simulated annealing protocol was used to test for compatibility of the constraints. All of the experimental spinach NOE constraints could be successfully combined with the E. coli data, confirming the general hypothesis of structural homology. A better fit was obtained with one form, suggesting a preferential stabilization of that form in the spinach case. Proteins 27:131-143 © 1997 Wiley-Liss, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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    Paper (German National Licenses)
  • 2
    Electronic Resource
    Electronic Resource
    In memoriam Yata Haneda (1995)
    New York : Wiley-Blackwell
    Journal of Bioluminescence and Chemiluminescence 10 (1995), S. 323-323 
    Details
    ISSN: 0884-3996
    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/bio.1170100602
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  • 3
    Electronic Resource
    Electronic Resource
    Copper binding and release by immobilized transferrin: A new approach to heavy metal removal and recovery (1997)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 53 (1997), S. 01-09 
    Details
    ISSN: 0006-3592
    Keywords: transferrin ; conalbumin ; metalloprotein ; affinity chromatography ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Recently these laboratories have demonstrated that it is possible to use proteins as efficient, selective agents for heavy metal removal and recovery. In this study, transferrin was chemically bound to an insoluble support. The ability of immobilized transferrin to produce clean water was demonstrated. Copper loading was independent of feed concentration. The loaded copper could be readily eluted and concentrated into the gram per liter range. The mechanism of copper release was studied. It was shown that release was dependent on pH and the chelating ability of the stripping agent. Metal release occurred slowly at pH 〈 7. However, at low pH in the presence of a chelator, metal removal occurred much more efficiently. The binding constant of copper to immobilized transferrin was determined as a function of pH. This information was used to model metal binding and release to the protein/support matrix. © 1997 John Wiley & Sons, Inc.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    An autoclavable glucose biosensor for microbial fermentation monitoring and control (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 46 (1995), S. 514-524 
    Details
    ISSN: 0006-3592
    Keywords: glucose biosensor ; biosensor ; glucose oxidase ; cellulose binding domain (CBD) ; fermentation monitoring ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The design, construction, and characterization of a prototype-regenerable glucose biosensor based on the reversible immobilization of glucose oxidase (GOx) using cellulose binding domain (CBD) technology is described. GOx, chemically linked to CBD, is immobilized by binding to a cellulose matrix on the sensor-indicating electode. Enzyme immobilization can be reversed by perfusing the cellulose matrix with a suitable eluting solution. An autocavable sensor membrane system is employed which is shown to be practical for use in real microbial fermentations. The prototype glucose biosensor was used without failure or deterioration during fed-batch fermentations of Escherichia coli reaching a maximum cell density of 85 g (dry weight)/L. Medium glucose concentration based on sensor output correlated closely with off-line glucose analysis and was controlled manually at 0.44 ± 0.2 g/L for 2 h based on glucose sensor output. The sensor enzyme component could be eluted and replaced without interrupting the fermentation. To our knowledge, no other in situ biosensor has been used for such an extended period of time in such a high-cell-density fermentation. © 1995 John Wiley & Sons, Inc.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260460604
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  • 5
    Electronic Resource
    Electronic Resource
    Immobilization of conalbumin onto polystyrene/divinylbenzene co-polymers: Towards finding the best support for MAMC (1996)
    Chicester [u.a.] : Wiley-Blackwell
    Journal of Molecular Recognition 9 (1996), S. 558-563 
    Details
    ISSN: 0952-3499
    Keywords: conalbumin ; affinity chromatography ; metal ; metalloprotein ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Immediately after the successful immobilization of conalbumin onto CNBr-activated Sepharose, efforts were begun to find a less expensive support and a more benign chemistry of activation. The potential of the Sepharose-conalbumin conjugate for decontamination of several metal-containing waste-waters has been established, and a new method of chromatography has emerged, named metalloprotein affinity metal chromatography (MAMC). Efforts to immobilize conalbumin onto polystyrene/divinylbenzene co-polymers, using the well known and commercially available Merrifield, aminomethyl and plain polystyrene resins are presented here. Immobilizations of conalbumin were carried out on the Merrifield and Aminomethyl resins, but the procedures were time consuming and complicated by polymer aggregation. Because of high cost of these materials, research was directed towards the activation and functionalization of plain polystyrene/divinylbenzene co-polymers. Chlorosulfonation followed by sulfonamide formation was attempted on three commercially available polymers. Successful polysulfonamide formation was achieved with bislysine copper(II) acting as a diamine. Removal of the copper allows the unblocking of the α amino group of the immobilized lysine which in turn is treated with glutaraldehyde, afforing an activated support for immobilization of proteins. To date, approximately 46 mg transferrin/g dry matrix have been successfully immobilized. The chemical and biological inertness of this support makes it a good candidate to scale up the procedure and continue the optimization of MAMC.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Metal ion concentration, time, and pH dependence of metal ion binding to a transferrin metalloprotein affinity chromatography (MAMC) matrix (1995)
    Chichester : Wiley-Blackwell
    Journal of Chemical Technology AND Biotechnology 64 (1995), S. 96-100 
    Details
    ISSN: 0268-2575
    Keywords: transferring ; conalbumin ; adsorption isotherms ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: The adsorption of transition metal, lanthanide, and actinide ions to avotransferrin (conalbumin) immobilized to sepharose (via the cyanogen bromide method) has been examined. Adsorption of ions as a function of time and adsorption isotherms at pH 8 have been determined and analyzed using the Freundlich model, distribution coefficients between the pH vales 2 and 9 have been measured. The results indicate that immobilization of the protein has little effect on its interactions with metal ions compared with the protein in solution, and important prerequisite for use of this matrix in metalprotein affinity metal homatography (MAMC).
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jctb.280640115
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  • 7
    Electronic Resource
    Electronic Resource
    Mechanism of lysosome rupture by dipeptides (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Cell Biochemistry and Function 13 (1995), S. 79-83 
    Details
    ISSN: 0263-6484
    Keywords: Lysosome membrane ; dipeptide ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Low concentrations of some neutral dipeptides, such as L-Ala-L-Ala, rapidly disrupt rat liver lysosmes. The phenomenon has been attributed to an osmotic imbalance generated by the production of amino acids in the lysosme by lysosomal dipeptidase activity. This hypothesis is challenged by testing several pairs of dipeptides available in both D- and L-forms and a range of dipeptides whose susceptibility to lysosomal dipeptidase activity is known. A good correlation was found between the lytic ability of dipeptides and their capacity to cross the lysosome membrane and be hydrolysed by lysosomal dipeptidase. The osmotic-imbalance hypothesis is critically evaluated in the light of the results and of recent information concerning the carrier-mediated transport of amino acids and dipeptides across the lysosome membrane. It is concluded that intralysosomal generation of amino acids remains the most plausible explanation of the lytic activity of dipeptides, and that the dipeptide proter(s) in the lysosome membrane must have higher Km than the amino acid porters.
    Additional Material: 3 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cbf.290130203
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  • 8
    Electronic Resource
    Electronic Resource
    Transferrin metalloprotein affinity metal chromatography (1995)
    Chichester : Wiley-Blackwell
    Journal of Chemical Technology AND Biotechnology 62 (1995), S. 373-379 
    Details
    ISSN: 0268-2575
    Keywords: transferrin ; affinity chromatography ; metalloprotein ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: The metal transport protein transferrin, when immobilized to Sepharose, can serve as an affinity media for the selective removal and subsequent release of heavy metal ions from aqueous solution. The material is stable over the pH range of 2-10, is self-indicating for the binding of certain metal ions, and maintains its integrity towards metal-binding capacity for long periods of time. In one step heavy metal ion concentrations can be reduced by at least five orders of magnitude to, at most, part per billion levels. The findings here presented suggest a novel practical method for the decontamination and/or recovery of metals ions from very dilute solutions and represent the first efforts to extend the concept of affinity chromatography to metal ions.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jctb.280620410
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  • 9
    Electronic Resource
    Electronic Resource
    Use of thermolysin metalloprotein affinity metal chromatography in the decontamination of actinide-bearing solutions (1995)
    Chichester : Wiley-Blackwell
    Journal of Chemical Technology AND Biotechnology 64 (1995), S. 149-152 
    Details
    ISSN: 0268-2575
    Keywords: thermolysin ; affinity chromatography ; metalloprotein ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Thermolysin metalloprotein affinity metal chromatography (MAMC) has been shown to be effective for the removal and concentration of lanthanide and actinide ions from aqueous solution. Using solution of trivalent lanthanide ions of appropriate radii and of Th4+ and UO22+ ions as models, the calciumbinding sites of immobilized thermolysin have shown appreciable potential for the decontamination of actinide-bearing waster solutions. The zinc-binding site of the affixed protein may also be used for the removal and concentration of divalent transition metal ions.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jctb.280640206
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