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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 501 (1987), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 434 (1984), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 28 (1986), S. 256-268 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The influence of chemical modification on the initial specific activity, residual activity, and deactivation kinetics of various enzymes is analyzed using a series mechanism. This straightforward multistate sequential model presented is consistent with the enzyme deactivation data obtained from different fields. The enzymes are placed in five different categories depending on the effect of chemical modification on initial specific activity and residual activity or stability. Wherever possible, structure-function relationships are described for the enzymes in the different categories. The categorization provides one avenue that leads to further physical insights into enzyme deactivation processes and into the enzyme structure itself.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 28 (1986), S. 1277-1285 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A general model of enzyme deactivations involving unimolecular processes is introduced. For most mechanisms of this type, the parameters of the general model can be expressed in terms of actual physical parameters. The number of physical parameters that can be determined from the deactivation data cannot exceed the number of independent constants in the general model. When there is an excess of physical parameters, then some parameters must be determined from independent methods of analysis. If this is not possible, then some parameters must be left as lumped parameters or global parameters. The general form of the model can be useful in determining the number of independent, potentially active forms of the enzyme present during deactivation. Some exceptions to the general model are due to higher-order processes such as dissociation, autolysis, and biological contamination.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 30 (1987), S. 717-723 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A two-parameter deactivation model is proposed to describe the kinetics of activity stabilization for some enzymes. The single-step unimolecular mechanism exhibits non-first-order deactivation kinetics since the final enzyme state, E1 is not completely inactivated. The usefulness of the model is demonstrated by applying it to the inactivation of different enzymes. The influence of the concentration of active ester, ionic strength, and pH on the model parameters is examined during the inactivation of electric eel acetylcholinesterase.25 In general, inactivators would decrease the level of activity stabilization, α1, and increase the first-order inactivation rate constant, k1. The effect of protecting agents would be to increase α1 and to decrease k1.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 34 (1989), S. 916-925 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Traditionally, enzyme populations have been treated as if they were either homogenous, or heterogeneous with distinct and separable subpopulations. The microheterogeneity model, however, assumes that there is a continuous distribution of properties in the population. In the area of enzyme deactivation kinetics, this model describes the heterogeneous population as having a continuous distribution of activation energy of deactivation. This distribution is characterized by mean activation energy, and a standard deviation of activation energy. The microheterogeneity model contains two parameters, ∊0 and σ. Parameter ∊0 is the mean value of ∊ for a heterogeneous enzyme population; ∊ is the activation energy divided by absolute temperature and the ideal gas constant. Parameter σ is the standard deviation of the Gaussian distribution of ∊ values in the population. If the population is homogeneous, then ∊ = ∊0 for all enzyme molecules and σ = 0. There are certain ratios which are independent of ∊0 and dependent upon σ. Two important ratios are t1/4/t1/2 and t1/2/t1/2′, where t1/2′ represents t1/2 for a homogeneous enzyme population with the same mean ∊ (∊0), as the heterogeneous population. If there is experimental deactivation data for the heterogeneous population which is well behaved, the first ratio, t1/4/t1/2, can be determined by estimating the time in minutes at which the enzyme has lost 25% of its activity (t1/4), and the time in minutes at which the enzyme has lost 50% of its activity (t1/2), and then taking the ratio t1/4/t1/2. The corresponding value of σ can be estimated from a graph. The ratio t1/2/t1/2′ can be found directly as a function of t1/4/t1/2, and can be estimated from another graph. The value of ∊0 can then be calculated from the formulasgiven in the article.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 28 (1986), S. 977-987 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A series-type enzyme deactivation model is used to model and to quantitate some more complex enzyme deacti-vations. The influence of temperature, pH, immobilization, chemical modifier (inhibitor or protector), substrate, and metal ion on the inactivation kinetics and on the parameter values is examined. In some cases the influence of two parameters on enzyme inactivations is presented. This provides further physical insights into enzyme inactivation and stabilization processes.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 26 (1984), S. 959-969 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A series-type enzyme deactivation model is utilized to theoretically analyze and to quantify the effect of chemical modifier concentration on the eventual level of enzyme activity stabilization, α2. An increase in the concentration of phosphate ion and NADP increases α2 for the enzymes studied. One example of each enzyme deactivation is given wherein the introduction of chemical modifiers changes the deactivation mechanism from a single-step to a series-type mechanism, and from a series-type to a single-step mechanism. Simple empirical equations are proposed to quantify the effect of chemical modifier concentration on α2.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 9
    Publication Date: 1984-01-01
    Print ISSN: 0141-0229
    Electronic ISSN: 1879-0909
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Published by Elsevier
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  • 10
    Publication Date: 1985-02-01
    Print ISSN: 0141-0229
    Electronic ISSN: 1879-0909
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Published by Elsevier
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