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  • Life and Medical Sciences  (518)
  • Biochemistry and Biotechnology  (221)
  • Wiley-Blackwell  (739)
  • 1985-1989  (739)
  • 1
    Electronic Resource
    Electronic Resource
    Laboratory studies on the suitability of a fertilizer-tap water medium for mass culture of algae (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 27 (1985), S. 1572-1576 
    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: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260271108
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  • 2
    Electronic Resource
    Electronic Resource
    An investigation of a fertilizer-tap water medium for mass algal production in outdoor plastic-enclosed systems (1987)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 30 (1987), S. 153-156 
    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 feasibility of using two fertilizers (urea plus superphosphate) in tap water as a medium for the mass culture of green algae (Scenedesmus and Ankistrodesmus) in outdoor plastic-enclosed minipond systems was investigated. Experiments in which the basic fertilizer-tap water medium was enriched with micro- and/or macronutrients revealed no nutrient deficiency symptoms in the algal biomass produced. Biomass production was found to be quantitatively related to the concentration of fertilizer added and maximal production (〉 15 g/m2 day) was achieved following the addition of 30 mg N/L (1.89 g N/m2 day) and 4.5 mg P/L (0.28 g P/m2/day).
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260300202
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  • 3
    Electronic Resource
    Electronic Resource
    Enhanced sedimentation of mammalian cells following acoustic aggregation (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 34 (1989), S. 559-562 
    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: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260340415
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  • 4
    Electronic Resource
    Electronic Resource
    Pharmacological profile of the substituted beta-lactam L-659,286: A member of a new class of human PMN elastase inhibitors (1989)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 39 (1989), S. 47-53 
    Details
    ISSN: 0730-2312
    Keywords: elastase inhibitors ; β-lactams ; lung damage ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Human polymorphonuclear leukocyte elastase (PMN elastase) is inhibited by L-659, 286 (7α-methoxy-8-oxo-3-[[(1,2,5,6-tetrahydro-2-methyl-5,6-dioxo-1,2,4-triaz-in-3-yl)thio]methyl]-5-thia-1-aza-6R-bicyclo [4.2.O]oct-2-ene-2-pyrrolidine carboxamide-5,-dioxide) with a Ki of 0.4 μM. This inhibition is time-dependent, rapid, and only slowly reversible, with a t1/2 of 〉 3 days at 25°C. L-659, 286 is also highly selective for PMN elastase, as it does not inhibit thrombin, trypsin, papain, plasmin, chymotrypsin, or cathepsin G. L-659, 286 administered intratracheally inhibits lung damage caused by administration via the same route of human PMN elastase into hamsters. In marmosets, L-659, 286 is cleared from blood very rapidly after an intravenous injection but is recovered in bronchoalveolar lavage fluid for several hours after intratracheal administration.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240390106
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  • 5
    Electronic Resource
    Electronic Resource
    Plant tubulin genes: Structure and differential expression during development (1987)
    Chichester [u.a.] : Wiley-Blackwell
    Developmental Genetics 8 (1987), S. 435-460 
    Details
    ISSN: 0192-253X
    Keywords: tubulin genes ; microtubules ; Arabidopsis thaliana ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Microtubules are important components of the cytoskeleton of plant cells and play key roles in plant growth and morphogenesis. Recent molecular studies have begun to elucidate the structure and expression of plant genes coding for the major components of microtubules, α- and β-tubulin. Tubulin amino acid sequences deduced from the DNA sequences of eight higher plant tubulin genes are 79-87% homologous with constitutively expressed mammalian tubulins. The genome of the model plant system Arabidopsis thaliana contains four dispersed α-tubulin sequences and at least seven β-tubulin sequences, only two of which appear to be linked. Of the five A. thaliana genes whose expression has been analyzed, the transcripts of one α-tubulin and one β-tubulin gene are constitutively expressed in roots, leaves, and flowers. A second α-tubulin gene is expressed predominately in flowers; the transcripts of the second and third β-tubulin genes are found predominately in leaves or in roots, respectively.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/dvg.1020080511
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  • 6
    Electronic Resource
    Electronic Resource
    Lymph heart musculature in birds (1987)
    New York, NY : Wiley-Blackwell
    Journal of Morphology 191 (1987), S. 77-87 
    Details
    ISSN: 0362-2525
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Development and innervation of the lymph heart musculature of chicken, emu, rhea, and duck was studied by electron microscopy at posthatch ages from 3 days to adulthood. Development of innervation was monitored by acetylcholinesterase staining. Horseradish peroxidase was used to determine the extent of the transverse tubule network. Chickens were unusual among these birds in that lymph heart myocytes had already undergone a definitive differentiation and degeneration by 3 days. In ducks and ratite birds, lymph heart myocytes more slowly but progressively differentiate a cytomorphology that does not conform in all characteristics to cardiac or skeletal muscle and even resembles in some aspects, smooth muscle. Myofibrils become the dominant cytoplasmic structure, transverse tubules form ‘internal couplings’ with agranular reticulum cisternae, and ‘external couplings’ are formed between myocytes at myomyal junctions. The myomyal junctions also contain AChE-positive reaction product and some subplasmalemmal vesicles that lack a dense core. The lymph heart myocardium of ducks of 2 weeks demonstrated mitotic figures. In adult ducks the myosatellite cell numbers diminish and a characteristic pattern of myocyte degeneration appears. In juvenile ducks and ratites some myocytes differentiate to conductile cells, much as the conductile myocytes and myofibers of the blood heart. The lymph heart innervation is described, and the role of nerve in differentiation and maintenance of myocyte morphology in the lymph heart is discussed.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jmor.1051910108
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  • 7
    Electronic Resource
    Electronic Resource
    Use of cell affinity chromatography for separation of lymphocyte subpopulations (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 27 (1985), S. 603-612 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: We describe the use of affinity chromatography for separation of cell populations that do not differ significantly with respect to gross physical properties such as size, density, or charge. Cell affinity chromatography exploits differences in cell surface macromolecules by passage of mixtures of cell populations through a column containing beads to which are attached chemical ligands with specific binding affinity for particular cell surface receptors. In this article we focus on the application of this concept to separation of mature T lymphocytes from peripheral blood. This serves as a model for the separation of these cells from bone marrow in order to prevent graft-vs.-host disease in bone marrow transplantation. However, the concept of cell affinity chromatography should find more general widespread utility in a variety of biotechnological applications. Thus, we introduce a simple theoretical framework which is necessary in order to understand the results that might be expected in any given situation. Finally, we use this theory to provide a tentative explanation for experimental observation of the effects of temperature and flowrate on the degree of separation achieved for our current pplication.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260270509
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  • 8
    Electronic Resource
    Electronic Resource
    Fundamental studies of glucose oxidase immobilization on controlled pore glass (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 27 (1985), S. 842-851 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Immobilization experiments have been performed with glucose oxidase as enzyme and controlled-pore glass of different pore sizes as support for chemical coupling. The experimental results have been analyzed for comparison with the theoretical model predictions. Analysis of the initial stage of the process gives the fundamental characteristic of the immobilization reaction. These investigations allow us to study the influence of the degree of diffusional restriction on the evolution of the immobilization process and spatial distribution of immobilized enzyme. Nonuniformly distributed concentrations have been achieved within the porous matrix, and suggestions have been made in designing such profiles by choosing appropriate experimental parameters.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260270614
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  • 9
    Electronic Resource
    Electronic Resource
    Modeling of enzyme immobilization in porous membranes (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 27 (1985), S. 1126-1135 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: This article deals with the mathematical modeling of the process of enzyme immobilization in porous membranes. During the initial period, an analytical solution is available to extract the rate constant for immobilization. Beyond this period, the model equations are solved numerically to yield the transient response of the enzyme concentration in the immobilizing solution and also the evolution of the enzyme loading profile inside the membrane. It is found that the immobilization practically ceases even through the attachment sites are still available within the membrane.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260270807
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  • 10
    Electronic Resource
    Electronic Resource
    A novel method of determination of the internal enzyme distribution within porous solid supports and the deactivation rate constant (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 28 (1986), S. 486-493 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: This article presents a method for determining the rate constant for deactivation and the internal distribution of immobilized enzyme. This method makes use of the parallel deactivation process in a diffusion-controlled regime, in which the internal activity profile behaves like a penetration front. This front basically traces through the initial active enzymatic profile, and one can determine the internal profile and the rate constant for deactivation from the experimentally observable bulk concentration versus time. This method is applied to the experimental data of the system of hydrogen-peroxide-immobilized catalase on controlled pore glass and Si-Al particles.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260280404
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