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  • General Chemistry  (99)
  • Biochemistry and Biotechnology  (98)
  • 2010-2014
  • 2000-2004
  • 1995-1999  (197)
  • 1955-1959
  • 1950-1954
  • 1997  (197)
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  • 2010-2014
  • 2000-2004
  • 1995-1999  (197)
  • 1955-1959
  • 1950-1954
Year
  • 1
    Electronic Resource
    Electronic Resource
    An activity coefficient model for proteins (1997)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 55 (1997), S. 940-940 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: No abstract.
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  • 2
    Electronic Resource
    Electronic Resource
    Tc(VII) reduction and accumulation by immobilized cells of Escherichia coli (1997)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 55 (1997), S. 505-510 
    Details
    ISSN: 0006-3592
    Keywords: bioreduction ; bioaccumulation ; immobilized cells ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Resting cells of Escherichia coli, immobilized in a flow-through bioreactor, coupled the oxidation of formate or hydrogen to Tc(VII) reduction and removal from solution. Cells, pregrown anaerobically in a hollow-fiber membrane bioreactor, were challenged with 50 μM Tc(VII) in a carrier solution of phosphate-buffered saline. The radionuclide accumulated within the membrane component of the reactor, corresponding to the localization of the cells. Negligible Tc removal was noted in a reactor containing a mutant deficient in active Tc(VII) reductase, when supplied with formate as an electron donor. Formate or hydrogen was supplied as the electron donor for Tc(VII) reduction to cells immobilized in reactors operated in transverse (crossflow) and direct (dead-end filtration) modes, respectively. Flow-rate activity relationships were used to compare the performance of the reactors. A flow rate of 2.4 mL h-1 supported the removal of 50% of the Tc from solution in a reactor operated in transverse mode with formate as an electron donor. In contrast, a flow rate of 0.7 mL h-1, supported comparable Tc removal when hydrogen was introduced to a reactor operated in direct mode. The reduced reactor efficiency, when hydrogen was used as an electron donor, could be attributed, in part, to poor delivery of the gas to the cells. The biocatalyst was highly stable in the reactor; no loss in activity was noted over 200 h of continuous use. © 1997 John Wiley & Sons Inc. Biotechnol Bioeng 55: 505-510, 1997.
    Additional Material: 5 Ill.
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  • 3
    Electronic Resource
    Electronic Resource
    An activity coefficient model for proteins (1997)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 55 (1997), S. 65-71 
    Details
    ISSN: 0006-3592
    Keywords: protein ; osmotic pressure ; activity coefficient ; solubility ; virial expansion ; UNIQUAC model ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Modeling of the properties of biochemical components is gaining increasing interest due to its potential for further application within the area of biochemical process development. Generally protein solution properties such as protein solubility are expressed through component activity coefficients which are studied here. The original UNIQUAC model is chosen for the representation of protein activity coefficients and, to the best of our knowledge, this is the first time it has been directly applied to protein solutions. Ten different protein-salt-water systems with four different proteins, serum albumin, alphacymotrypsin, beta-lactoglobulin and ovalbumin, are investigated. A root-mean-squared deviation of 0.54% is obtained for the model by comparing calculated protein activity coefficients and protein activity coefficients deduced from osmotic measurements through virial expansion. Model predictions are used to analyze the effect of salt concentrations, pH, salt types, and temperature on protein activity coefficients and also on protein solubility and demonstrate consistency with results from other references. © 1997 John Wiley & Sons, Inc. Biotechnol Bioeng 55: 65-71, 1997.
    Additional Material: 3 Ill.
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  • 4
    Electronic Resource
    Electronic Resource
    Biological breakdown of RDX in slurry reactors proceeds with multiple kinetically distinguishable paths (1997)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 56 (1997), S. 258-267 
    Details
    ISSN: 0006-3592
    Keywords: RDX biotransformation ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Biotransformation of RDX (hexahydro-1,3,5-trinitro-1,3,5-triazine) in slurry reactors was studied to determine the importance of supplementation of known biodegraders and the type of nutrient source required. Although addition of bacteria to the system increased the biotransformation rates, the increase may not justify the additional work and cost needed to grow the organisms in a laboratory and mix them into the soil. An inexpensive, rich nutrient source, corn steep liquor, was shown to provide sufficient nutrients to allow for the cometabolic biotransformation of RDX. The rate of RDX transformation was not constant throughout the course of the experiment due to the heterogeneous microbial population. Three kinetically distinct phases were observed. Regardless of the process, RDX biotransformation in slurry reactors was reaction rate limited under the test conditions. Model simulations based on experimental results demonstrate that, at cell densities of 5 g/L, bioremediation of RDX-contaminated soil is an attractive clean-up alternative. © 1997 John Wiley & Sons, Inc. Biotechnol Bioeng 56: 258-267, 1997.
    Additional Material: 7 Ill.
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  • 5
    Electronic Resource
    Electronic Resource
    [(TptBu, Me)CrR]: A New Class of Mononuclear, Coordinatively Unsaturated Chromium(II) Alkyls with cis-Divacant Octahedral Structure (1997)
    Weinheim : Wiley-Blackwell
    Chemistry - A European Journal 3 (1997), S. 1668-1674 
    Details
    ISSN: 0947-6539
    Keywords: alkenes ; chromium ; cis-divacant octahedral geometry ; polymerizations ; tris(pyrazolyl)borate complexes ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Reaction of CrCl2 with TptBu, MeK yielded [TptBu, MeCr(3-tBu, 5-MepzH)Cl] (1) and [TptBu, MeCrCl] (2), while the same reaction in the presence of pyridine gave 1 and [TptBu, MeCr(py)Cl] (3). Alkylation of 3 with Grignard reagents produced the chromium(II) alkyls [TptBu, MeCrR] (4, R = Et; 5, R = Ph; 6, R = CH2SiMe3), which reversibly added to pyridine to form the five-coordinate adducts [TptBu, MeCr(py)R] (7, R = Et; 8, R = Ph; 9, R = CH2SiMe3). 1, 2, 4, and 5 were structurally characterized by X-ray diffraction. The four-coordinate molecules 2, 4, and 5 adopt a highly unusual cis-divacant octahedral coordination geometry, while 1 is the first five-coordinate TptBu, Me-complex of a first-row transition metal. Despite their coordinative unsaturation, chromium alkyls 4-6 do not polymerize ethylene, or even react with it. This observation is inconsistent with the catalytic activity commonly ascribed to divalent chromium in heterogeneous polymerization catalysts. Attempts to oxidize 4-6 (e.g., with [Cp2Fe]BPh4) to cationic chromium(II) alkyls failed, yielding [TptBu, MeCr(thf)][BPh4] (10) instead.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/chem.19970031016
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  • 6
    Electronic Resource
    Electronic Resource
    ‘Proteomic contigs’ of Mycobacterium tuberculosis and Mycobacterium bovis (BCG) using novel immobilised pH gradients (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 1384-1392 
    Details
    ISSN: 0173-0835
    Keywords: Two-dimensional polyacrylamide gel electrophoresis ; Proteome ; Mycobacterium tuberculosis ; Mycobacterium bovis (BCG) ; Immobilised pH gradient ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Tuberculosis remains a major health problem throughout the world and the failure of the existing bacille Calmette-Guérin (BCG) vaccine in recent trials has prompted a search for potential replacements. Recent advances in molecular and cell biology have cast doubts on the ability of genetic analysis alone to predict polygenic human diseases and other complex phenotypes and have therefore redirected our attention to proteome studies to complement information obtained from DNA sequencing initiatives. Novel acidic (pH 2.3-5) and basic (pH 6-11) IPG gel gradients were employed in conjunction with commercially available pH 4-7 gradients to significantly increase (fourfold) the number of protein spots previously resolved on two-dimensional (2-D) gels of Mycobacterium species. A total of 772 and 638 protein spots were observed for M. bovis BCG and M. tuberculosis H37Rv, respectively, the latter corresponding to only the pH regions 4-7 and 6-11. Of interest was the bimodal distribution observed for proteins separated from M. bovis BCG across both Mr and pH ranges. Some differences in protein expression were observed between these two organisms, contrary to what may have been expected considering the high degree of conservation in gene order and sequence similarity between homologous genes. Further work will be directed towards a more detailed analysis of these differences, so as to allow more accurate diagnosis between vaccination and active tuberculosis. The latter is of major importance to epidemiological studies and for patient management.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150180813
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  • 7
    Electronic Resource
    Electronic Resource
    Capillary electrophoresis-based separation of transferrin sialoforms in patients with carbohydrate-deficient glycoprotein syndrome (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 1819-1826 
    Details
    ISSN: 0173-0835
    Keywords: Carbohydrate-deficient transferrin ; Glycosylation ; Sialic acid ; Physical gel ; Sieving matrix ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The heterogeneity associated with protein glycoforms has been a challenge to analytical chemists and the subject of structure-function studies for biochemists since their presence in biological systems had been confirmed some three decades ago. Initial investigations led to discoveries of synthetic and degradative pathways, and brief forays into functional determination of the “glyco” portion on the protein activity in glycoproteins. Only recently has it come to our understanding that variations from the “normal” glycosylation patterns might be indicative of pathological states. The presence of certain transferrin (Tf) glycoforms in human serum has been shown to correlate with certain clinical syndromes. Hence, the ability to separate and quantitatively measure the various forms of human Tf has become increasingly important. It this study, we demonstrate that a simple method utilizing a DB-17-coated capillary to slow endoosmotic flow and a sieving buffer containing hydroxyethyl cellulose allows for the resolution of sialoforms of transferrin. An analysis time of less than eight minutes allows for baseline resolution of the lower sialoforms of Tf, presenting a simple, rapid test for carbohydrate-deficient transferrin (CDT). We demonstrate the utility of this methodology for the facile diagnosis of carbohydrate-deficient glycoprotein syndrome, and postulate that it may allow for the detection of other carbohydrate-deficient protein-related disease states.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150181017
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  • 8
    Electronic Resource
    Electronic Resource
    Prefractionation of protein samples prior to two-dimensional electrophoresis (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 317-323 
    Details
    ISSN: 0173-0835
    Keywords: Prefractionation ; Preparative electrophoresis ; Native electrophoresis ; Two-dimensional polyacrylamide gel electrophoresis ; Proteome ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Thousands of proteins may be visualised on a two-dimensional (2-D) gel, but only hundreds are present at levels sufficient for chemical analysis. Therefore, prefractionation of protein samples prior to 2-D polyacrylamide gel electrophoresis (PAGE) will be important for the investigation of proteins that are present at sub-picogram levels in physiological samples. We describe an approach to prefractionate protein samples prior to 2-D PAGE using the Gradiflow, which is a new (preparative) electrokinetic membrane apparatus designed to fractionate proteins in a number of different ways. We have fractionated human serum under nonreducing conditions using the ‘reflux’ mode, in which proteins are fractionated according to their relative mobility under controlled electrophoretic conditions, where the current is periodically reversed. We describe how fractionation occurs and present examples of enrichment of specific proteins.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150180304
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  • 9
    Electronic Resource
    Electronic Resource
    Production of recombinant bacterial endoglucanase as a co-product with ethanol during fermentation using derivatives of Escherichia coli KO11 (1997)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 55 (1997), S. 547-555 
    Details
    ISSN: 0006-3592
    Keywords: ethanol ; cellulose ; hemicellulose ; endoglucanase ; cellulase ; lignocellulose ; biomass ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: This study demonstrates a new approach to reduce the amount of fungal cellulase required for the conversion of cellulose into ethanol. Escherichia coli KO11, a biocatalyst developed for the fermentation of hemicellulose syrups, was used to produce recombinant endoglucanase as a co-product with ethanol. Seven different bacterial genes were expressed from plasmids in KO11. All produced cell-associated endoglucanase activity. KO11(pLOI1620) containing Erwinia chrysanthemi celZ (EGZ) produced the highest activity, 3,200 IU endoglucanase/L fermentation broth (assayed at pH 5.2 and 35°C). Recombinant EGZ was solubilized from harvested cells by treatment with dilute sodium dodecyl sulfate (12.5 mg/ml, 10 min, 50°C) and tested in fermentation experiments with commercial fungal cellulase (5 filter paper units/g cellulose) and purified cellulose (100 g/L). Using Klebsiella oxytoca P2 as the biocatalyst, fermentations supplemented with EGZ as a detergent-lysate of KO11(pLOI1620) produced 14%-24% more ethanol than control fermentations supplemented with a detergent-lysate of KO11(pUC18). These results demonstrate that recombinant bacterial endoglucanase can function with fungal cellulase to increase ethanol yield during the simultaneous saccharification and fermentation of cellulose. © 1997 Wiley & Sons, Inc. Biotechnol Bioeng 55: 547-555, 1997.
    Additional Material: 4 Ill.
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  • 10
    Electronic Resource
    Electronic Resource
    A novel membrane reactor design for controlled studies of interacting populations (simulation of the interaction between microorganism and plant suspension cultures) (1997)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 55 (1997), S. 609-615 
    Details
    ISSN: 0006-3592
    Keywords: interacting populations ; membrane reactor ; induced metabolic changes ; elicitation ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The design of a reactor in which two interacting cell populations (microorganisms and plants) could grow under controlled conditions was considered. In this reactor, the cell populations are separated by a membrane which permits semi-in vivo study of induced interaction-specific changes in metabolism. In this paper, the interaction of suspension culture of Nicotiana tabacum (tobacco) and the Oomycete, Phytophthora nicotiana was simulated. The results of the computer simulation show the induced metabolic changes as a consequence of the biological interaction. The paper introduces a novel approach in the strategy for the study of interacting population in suspension cultures. This type of system has potential applications in studies of the regulation of secondary metabolism and for the production of high values pharmaceuticals. © 1997 John Wiley & Sons, Inc. Biotechnol Bioeng 55: 609-615, 1997.
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