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  • 1
    Electronic Resource
    Electronic Resource
    Effects of plasmid presence on growth and enzyme activity of Escherichia coli DH5α (1989)
    Springer
    Applied microbiology and biotechnology 32 (1989), S. 54-60 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary The effects of recombinant DNA propagation and gene expression on the physiology of the host cell was investigated using a series of copy number mutant plasmids. The plasmids at copy numbers of 30, 57, 115 and 501 per chromosome equivalent encoded constitutive production of the enzyme β-lactamase. Ribose phosphate isomerase activity was relatively unaffected by plasmid presence, and glucose-6-phosphate dehydrogenase, fructose 1,6-diphosphate aldolase and fructose 1,6-diphosphatase activities were lower in plasmid-containing cells than in the plasmid-free host strain. Increasing copy number resulted in increased depression of enzyme activity levels. The results indicate that plasmid presence mediates subtle changes in the net expression of host enzymes involved in carbon metabolism. Responses of Escherichia coli DH5α in Evans medium to these plasmids differed substantially from responses of E. coli HB101 in rich medium.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00164823
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  • 2
    Electronic Resource
    Electronic Resource
    The pharmacokinetics of volatile anesthetic agent elimination: A theoretical study (1989)
    Springer
    Journal of pharmacokinetics and pharmacodynamics 17 (1989), S. 109-123 
    Details
    ISSN: 1573-8744
    Keywords: anesthetics, gases ; pharmacokinetics ; volatile anesthetics ; inhalation agents
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The theoretical groundwork for a rate constant formulation of inhaled anesthetic elimination kinetics is discussed. In an effort to simulate recent experimental results a linear flow-limited five-compartment model was used comprising lung, vessel-rich tissue, muscle, nonvisceral fat, and an additional compartment, marrow-visceral fat whose functional existence recently has been experimentally demonstrated. Hypothetical but plausible parameters for the marrow-visceral fat compartment were used. The theoretically predicted values were in good agreement with experimental results suggesting that this model is appropriate for the elimination kinetics of agents that are not metabolized to any significant degree. Simple approximate expressions for the rate constants were also derived and were in reasonable agreement with experimental results. The model was also employed to clarify the effect of anesthetic duration on subsequent elimination kinetics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01059090
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  • 3
    Electronic Resource
    Electronic Resource
    Aggregation kinetics in salt-induced protein precipitation (1989)
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 35 (1989), S. 1779-1790 
    Details
    ISSN: 0001-1541
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The kinetics of protein aggregation in salt-induced precipitation processes were studied as a function of salt type, salt concentration, temperature and protein concentration. α-chymotrypsin (αCT) was used as a model protein. Stopped-flow turbidimetry was used to monitor the progress of precipitations. Analysis of the linear portions of the turbidity trajectories indicates that temperature and salt concentration effects are related to protein solubility; the protein concentration dependence is well described by the Smoluchowski collision equation. The aggregation kinetics of partially-inhibited αCT exhibit poisoning behavior, underscoring the importance of dimerization and monomer addition in the precipitation of αCT. Solute particle radius distributions determined via dynamic laser light scattering for low salt and supernatant αCT solutions indicated that significant aggregation does not occur in the absence of supersaturation. A detailed population balance model was proposed that accounted for specific and nonspecific interactions and monomer addition. The model is expected to find general application to protein aggregation phenomena, in particular for proteins that have specific quaternary interactions.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aic.690351104
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  • 4
    Electronic Resource
    Electronic Resource
    Effects of pH and added metabolites on bioconversions by immobilized non-growing Clostridium acetobutylicum (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 34 (1989), S. 825-837 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The bioconversion activity of calcium alginate-immobilized Clostridium acetobutylicum ATCC 824 was investigated in a continuous reactor system utilizing a defined feed medium which did not support cell growth. The changes in biocatalytic activity with time were studied at different pH values as well as when different metabolites (butyric, acetic, and acetoacetic acids) were present in the feed stream. Although the nongrowing cells were metabolically active, the product distribution was shifted from solvent production to acidogenesis. Overall activity losses occurred due to cell lysis, sporulation, and the effects of nitrogen level on macromolecular turnover. These effects were minimized under some operating conditions (e.g., pH 6), resulting in significantly longer productivity lifetimes.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260340612
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  • 5
    Electronic Resource
    Electronic Resource
    Alteration of substrate regulation patterns in glutamate dehydrogenase by enzyme immobilization (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 33 (1989), S. 896-905 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Substrate regulation patterns were changed by covalent binding of bovine liver glutamate dehydrogenase via primary amino groups to CNBr- and CH-activated Sepharose 4B. Lineweaver-Burk plots show that the NAD activation region changed from being abrupt to elongated when the enzyme was immobilized to either support. The elongated region contains two inflection points and resembles substrate activation of several other allosteric oligomers. Glutamate induced varying degrees of abrupt activation in immobilized glutamate dehydrogenase and inhibited the native enzyme. This activation is characterized by an activation threshold, an increase in the apparent dissociation constant, and a correlation between the apparent rate constant and the degree of activation. These three features characterize other glutamate dehydrogenase systems.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260330713
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  • 6
    Electronic Resource
    Electronic Resource
    In vivo nuclear magnetic resonance analysis of immobilization effects on glucose metabolism of yeast Saccharomyces cerevisiae (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 33 (1989), S. 1283-1289 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Fermentation rates and intracellular compositions have been determined for alginate-entrapped Saccharomyces cerevisiae and for identical cells in suspension. Glucose uptake and ethanol and glycerol production are approximately two times faster in immobilized cells than in suspended cells. Phosphorus-31 nuclear magnetic resonance (NMR) spectroscopy of fermenting immobilized and suspended cells shows differences in intermediate metabolite levels such as fructose-1,6 diphosphate, glucose-6-phosphate, and 3-phosphoglycerate and in internal pH. Carbon-13 NMR shows an increase in polysaccharide production. These data suggest that immobilization has accelerated the rate of glucose transport or of glucose phosphorylation. These effects of immobilization upon cell metabolism are observed in a very short period of time under conditions in which negligible DNA, RNA, or protein synthesis takes place.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260331009
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  • 7
    Electronic Resource
    Electronic Resource
    ESR investigations of free and immobilized glutamate dehydrogenase (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 34 (1989), S. 110-116 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The structure of bovine liver glutamate dehydrogenase was examined with 2,2,6,6-tetramethyl-4-oxopiperidine-1-oxyl (TEMPO I) and 4-((4-(chloromercurio)benzoyl) amino)-2, 2, 6, 6-tetramethyl-1-piperidinyloxy (TEMPO II). ESR spectra from TEMPO I show that enzyme structure in the vicinity of this spin label was not distorted during immobilization to a Sepharose support. Deactivation studies with pyridoxal 5′-phosphate indicate that immobilization did not expose additional binding sites to TEMPO I. Spectra from TEMPO II reveal that immobilization profoundly altered conformational change induced by α-ketoglutarate and suppressed that induced by GTP and NADPH. This structural investigation provides insight into the altered kinetic properties of Sepharose-immobilized glutamate dehydrogenase and suggests a fundamental difference between monomers and allosteric oligomers in their structural response to immobilization.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260340114
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  • 8
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    Evidence for partial export of Vitreoscilla hemoglobin into the periplasmic space in Escherichia coli (1989)
    Elsevier
    Details
    Publication Date: 1989-11-01
    Print ISSN: 0022-2836
    Electronic ISSN: 1089-8638
    Topics: Biology
    Published by Elsevier
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  • 9
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    Structure-function relationships in the inorganic salt-induced precipitation of α-chymotrypsin (1989)
    Elsevier
    Details
    Publication Date: 1989-05-01
    Print ISSN: 0167-4838
    Electronic ISSN: 1879-2588
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Published by Elsevier
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  • 10
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    Solubility-activity relationships in the inorganic salt-induced precipitation of α-chymotrypsin (1989)
    Elsevier
    Details
    Publication Date: 1989-05-01
    Print ISSN: 0141-0229
    Electronic ISSN: 1879-0909
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Published by Elsevier
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