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  • Cell & Developmental Biology  (195)
  • FLUID MECHANICS AND HEAT TRANSFER  (140)
  • Biochemistry and Biotechnology  (100)
  • 1985-1989  (421)
  • 1970-1974
  • 1960-1964  (9)
  • 1935-1939  (1)
  • 1905-1909
  • 1890-1899  (4)
  • 1989  (237)
  • 1986  (184)
  • 1963  (9)
  • 1937  (1)
  • 1897  (3)
  • 1892  (1)
Collection
Keywords
Publisher
Years
  • 1985-1989  (421)
  • 1970-1974
  • 1960-1964  (9)
  • 1935-1939  (1)
  • 1905-1909
    • +
Year
  • 1
    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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    Paper (German National Licenses)
    Fulltext
  • 2
    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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    Paper (German National Licenses)
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  • 3
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    Laminar flow integration: Flight tests status and plans (1986)
    In:  CASI
    Details
    Publication Date: 2013-08-31
    Description: Under the Aircraft Energy Efficiency - Laminar Flow Control Program, there are currently three flight test programs under way to address critical issues concerning laminar flow technology application to commercial transports. The Leading-Edge Flight Test (LEFT) with a JetStar aircraft is a cooperative effort with the Ames/Dryden Flight Research Facility to provide operational experience with candidate leading-edge systems representative of those that might be used on a future transport. In the Variable Sweep Transition Flight Experiment (VSTFE), also a cooperative effort between Langley and Ames/Dryden, basic transition data on an F-14 wing with variable sweep will be obtained to provide a data base for laminar flow wing design. Finally, under contract to the Boeing Company, the acoustic environment on the wing of a 757 aircraft will be measured and the influence of engine noise on laminar flow determined with a natural laminar flow glove on the wing. The status and plans for these programs are reported.
    Keywords: FLUID MECHANICS AND HEAT TRANSFER
    Type: Langley Symposium on Aerodynamics, Volume 1; p 485-518
    Format: application/pdf
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    NASA TECHNICAL REPORTS
  • 4
    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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  • 5
    Electronic Resource
    Electronic Resource
    Effect of induction temperature on the production of malaria antigens in recombinant E. coli (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 34 (1989), S. 854-862 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: As part of a process development campaign, studies have been conducted to determine the influence of induction temperature on the expression of two different malaria antigens, RN1 and RT2. Single-step temperature inductions, in which growth at 32.0°C is followed by a shift in temperature to a desired setpoint, show that there exists an optimum duration and temperature of induction which is product specific. Between an induction temperature of 39.5 and 44.5°C RN1 yield is constant at ca. 0.20 g/g total soluble protein (TSP). RT2 yield approaches 0.20 g/g TSP only at elevated induction temperatures. The optimum temperature of induction for RN1 production is 39.5°C, whereas, that for RT2 production is 41.0°C. Above the optimum temperature of induction antigen concentration decreases owing to decreases in biomass. Furthermore, the maximum concentration of these two antigens differ by a factor of four. With increasing temperature of induction the extent of proteolysis of the products also appears to increase.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260340615
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  • 6
    Electronic Resource
    Electronic Resource
    Enzymatic production of long-chain aldehydes in a fixed bed reactor using organic solvents and cofactor regeneration (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 33 (1989), S. 229-232 
    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: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260330214
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  • 7
    Electronic Resource
    Electronic Resource
    On-line monitoring of cell mass in mammalian cell cultures by acoustic densitometry (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 33 (1989), S. 1379-1384 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Acoustic resonance densitometry (ARD) provides a highly reproducible and stable method for on-line measurement of culture biomass density. The technique provides a direct determination of changes in relative density of culture medium and cell mass. At cell concentrations higher than 106 cells mL-1this method can replace cell counts and provide a continuous measure of total cell mass. In cultures of hybridomas or U937 human lymphoma cells, the ARD value correlates well with cell number except when the average cell size changes during culture. It is argued that cell mass determined by ARD rather than cell number should be used as the basis for measurements of specific biological activity.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260331103
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  • 8
    Electronic Resource
    Electronic Resource
    General theory of determining intraparticle active immobilized enzyme distribution and rate parameters (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 33 (1989), S. 963-975 
    Details
    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 theory is presented in this article for determining the intrinsic rate constants for the main reaction and deactivation reaction, the effective diffusivity of the substrate, and the active enzyme distribution within porous solid supports from deactivation study of a continuous stirred-basket reactor (CSBR). For the parallel deactivation five reaction kinetics are considered: (a) Michaelis-Menten, (b) substrate inhibition, (c) product inhibition (competitive), (d) product inhibition (anticompetitive), and (e) zero-order kinetics. The experimental results of the system of hydrogen-peroxide-immobilized catalase on controlled-pore glass particles are analyzed to demonstrate the application of the theory developed for parallel deactivation of active immobilized enzyme (IME). For series deactivation only first-order kinetics is treated, and a numerical procedure is proposed to deter mine the rate parameters and the internal active enzyme distribution. The experimental data of the system of glucose-immobilized glucose oxidase on silica-alumina and controlled-pore glass particles are used to verify the theory.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260330805
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  • 9
    Electronic Resource
    Electronic Resource
    Direct evidence for a xylose metabolic pathway in Saccharomyces cerevisiae (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 28 (1986), S. 549-553 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Xylose transport, xylose reductase, and xylitol dehydrogenase activities are demonstrated in Saccharomyces cerevisiae. The enzymes in the xylose catabolic pathway necessary for the conversion of xylose to xylulose are present, although S. cerevisiae cannot grow on xylose as a sole carbon source. Xylose transport is less efficient than glucose transport, and its rate is dependent upon aeration. Xylose reductase appears to be a xylose inducible enzyme and xylitol dehydrogenase activity is constitutive, although both are repressed by glucose. Both xylose reductase and xylitol dehydrogenase activities are five- to tenfold lower in S. cerevisiae as compared to Candida utilis. In vivo conversion of 14C-xylose in S. cerevisiae is demonstrated and xylitol is detected, although no significant levels of any other 14C-labeled metabolites (e. g., ethanol) are observed.
    Additional Material: 4 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260280411
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  • 10
    Electronic Resource
    Electronic Resource
    Chemostat study of kinetics of human lymphokine synthesis in recombinant Escherichia coli (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 34 (1989), S. 415-421 
    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.260340318
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