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  • 1
    Electronic Resource
    Electronic Resource
    Whiskers, C. C. Evans, M & B Monograph Me/8, Mills and Boon, Ltd., London (1972). 72 pages. £1.5 (1972)
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 18 (1972), S. 1278-1278 
    Details
    ISSN: 0001-1541
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aic.690180639
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  • 2
    Electronic Resource
    Electronic Resource
    Flow of molten poly(ethylene terephthalate) through packed beds of glass beads (1972)
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 18 (1972), S. 443-445 
    Details
    ISSN: 0001-1541
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aic.690180233
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  • 3
    Electronic Resource
    Electronic Resource
    Impurity effects in continuous-flow mixed suspension crystallizersThe terms additive and impurity will be used interchangeably in this paper. (1973)
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 19 (1973), S. 510-516 
    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 crystallization of NaCl in the presence of Pb+ + as an Impurity in a continuous, mixed suspension, mixed product removal (CMSMPR) crystallizer was investigated. The results indicated that nucleation and growth rates as well as the dominant crystal sizes can be correlated by simple power functions of impurity concentration. The exponents are constants independent of the impurity concentration, thus permitting the prediction of nucleation rates, growth rates and size distributions at various concentrations of that impurity. This model was shown to apply also to other crystallizing systems.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aic.690190314
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  • 4
    Electronic Resource
    Electronic Resource
    A modeling study of anaerobic biofilm systems: I. Detailed biofilm modeling (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 46 (1995), S. 43-53 
    Details
    ISSN: 0006-3592
    Keywords: acetate ; anaerobic biofilms ; mass transfer ; pH ; biofilm modeling ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A detailed model acetate-utilizing methanogenic biofilms accounting for the diffusion of neutral and ionic species, chemical equilibrium, electroneutrality, gas production within the biofilm, pH-dependent Monod kinetics, and the presence of a concentration boundary layer is presented. The model qualitatively fits the pH profiles that are reported for acetate-utilizing methanogenic aggregates. A sensitivity analysis on the biological parameters showed that the flux of acetate is sensitive to the maximum utilization rate, half-saturation constant, and biofilm density for the bulk conditions investigated. Criteria when traditional biofilm models can be used to predict the flux of acetate into the biofilm are established. If the maximum pH change predicted using a hypothetical system is within ±0.05, the traditional model predicts the flux to within ±5% of the value calculated with the model developed in this study. © 1995 John Wiley & Sons, Inc.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260460107
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  • 5
    Electronic Resource
    Electronic Resource
    Recombinant production and purification of novel antisense antimicrobial peptide in Escherichia coli (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 57 (1998), S. 55-61 
    Details
    ISSN: 0006-3592
    Keywords: synthetic antimicrobial peptide ; prochymosin ; recombinant ; expression ; purification ; fusion protein ; inclusion bodies ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A fusion protein was genetically engineered that contains an antimicrobial peptide, designated P2, at its carboxy terminus and bovine prochymosin at its amino terminus. Bovine prochymosin was chosen as the fusion partner because of its complete insolubility in Escherichia coli, a property utilized to protect the cells from the toxic effects of the antimicrobial peptide. This fusion protein was purified by centrifugation as an insoluble inclusion body. A methionine linker between prochymosin and the P2 peptide enabled P2 to be released by digestion with cyanogen bromide. Cation exchange HPLC followed by reversed-phase HPLC were used to purify the P2 peptide. The recombinant P2 peptide's molecular mass was confirmed by mass spectrometry to within 0.1% of the theoretical value (2480.9 Da), and the antimicrobial activity of the purified recombinant P2 against E. coli D31 was determined to be identical to that of the chemically synthesized peptide (minimal inhibitory concentration of 5 mg/mL). Although the yield of the fusion protein after expression by the cells was high (16% of the total cell protein), the percentage recovery of the P2 peptide in the inclusion bodies was relatively low, which appears to be due to losses in the cyanogen bromide digestion step. © 1998 John Wiley & Sons, Inc. Biotechnol Bioeng 57: 55-61, 1998.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    A modeling study of anaerobic biofilm systems: II. Reactor modeling (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 46 (1995), S. 54-61 
    Details
    ISSN: 0006-3592
    Keywords: anaerobic biofilm ; CSTR ; reactors, nonide ; pH ; plug-flow reactors ; biofilm modeling ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A rigorous steady-state model of anaerobic biofilm reactors taking into account acid-base and gas-phase equilibria in the reactor in conjunction with detailed chemical equilibria and mass transfer in acetate-utilizing methanogenic biofilms is presented. The performances of ideal completely stirred tank reactors (CSTRs) and plug-flow reactors, as well as reactors with nonideal hydraulic conditions, are simulated. Decreasing the surface loading rate increases the acetate removal efficiency, while decreasing the influent pH and increasing the buffering capacity improves the removal efficiency only if the bulk pH of the reactor shifts toward more optimal values between 6.8 to 7.0. The reactor can have negative or positive removal efficiencies depending on the start-up conditions. The respiration coefficient plays a critical role in determining the minimum influent pH required for reactor recovery after failure. Having multiple CSTRs-in-series generally increases the overall removal efficiency for the influent conditions investigated. Monitoring of the influent feed quality is critical for plug-flow reactors, becasue failure of the initial sections of the reactor may cause a cascading effect that may lead to a rapid reactor failure. © 1995 John Wiley & Sons, Inc.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260460108
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  • 7
    Electronic Resource
    Electronic Resource
    Induction of autocrine epidermal growth factor receptor ligands in human keratinocytes by insulin/insulin-like growth factor-1 (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 163 (1995), S. 257-265 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Autocrine activation of the epidermal growth factor (EGF) receptor on keratinocytes has been recognized as an important growth regulatory mechanism involved in epithelial homeostasis, and, possibly, hyperproliferative diseases. Insulin-like growth factor (IGF)-1 and insulin have been shown to be paracrine keratinocyte mitogens that bind to the type I IGF receptor which is expressed on actively proliferating keratinocytes in situ. In this report, we demonstrate that IGF-1/insulin induced production of keratinocyte-derived autocrine growth factors that bind to the EGF receptor. Increased steady-state mRNA levels for transforming growth factor alpha (TGF-α) and for amphiregulin (AR) were observed upon incubation of keratinocytes with mitogenic concentrations of IGF-1. IGF-1 also induced production and secretion of TGF-α and AR proteins as detected by immunoassays. An EGF receptor antagonistic monoclonal antibody abolished the mitogenic effect of IGF-1 on cultured keratinocytes. These results suggest that stimulation of keratinocyte growth by IGF-1 requires activation of an EGF receptor-mediated autocrine loop. © 1995 Wiley-Liss, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041630206
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  • 8
    Electronic Resource
    Electronic Resource
    Heparin inhibition of autonomous growth implicates amphiregulin as an autocrine growth factor for normal human mammary epithelial cells (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 153 (1992), S. 103-111 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Normal human mammary epithelial cells (HMECs) proliferate in a serum-free defined growth medium in the absence of epidermal growth factor (Li and Shipley, 1991). Amphiregulin (AR) is a heparin-regulated, EGF-like growth factor. Our observation that one strain of HMECs produce AR mRNA (Cook et al., 1991a) stimulated us to determine whether AR expression was a common phenomenon in HMECs and whether AR could act as an autocrin growth factor to support the EGF-independent growth of these cells. In this study, we detected high levels of AR expression in four separate HMEC strains while one immortal mammary cell line (HBL-100) and six mammary tumor-derived cell lines had low to undetectable levels of AR. The EGF-indendent growth of HMECs was blocked by the addition of heparin or a monoclonal anti-RGF receptors antibody to the culture medium, implication AR as an autocrine growth mediator. This hypothesis is further supported by the fact that medium conditioned by HMECs contains secreted AR protein. A mammary tumor-derived cell line, Hs578T, which proliferates in an EGF-independent manner, does not express detectable levels of AR and is not growth inhibited by heparin. Examination of the same cell types for expression of transforming growth factor type-alpha (TGF-α) mRNA revealed coordinate expression of AR and TGF-α in these cells. These data suggest that both AR and TGF-α mRNA are produced in much greater abundance by normal HMECs than in tumor-derived cells in culture, and that AR is an important autostimulatory factor for the growth of normal HMECs. © 1992 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041530114
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  • 9
    Electronic Resource
    Electronic Resource
    Photoemission study of an AuPdAu(111) multilayer grown by MBE (1993)
    Chichester [u.a.] : Wiley-Blackwell
    Surface and Interface Analysis 20 (1993), S. 919-922 
    Details
    ISSN: 0142-2421
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Physics
    Notes: An au/Pd/Au(111) multilayer system grown by molecular beam epitaxy has been studied by high-resolution x-ray photoelectron spectroscopy. An analysis of the dependence of the relative intensity of the Au and Pd core-level XPS lines on the take-off angle indicates that the thickness of the Pd sandwhich layer is ∼5 monolayers. The photoelectron spectra show the presence of more than one chemical environment for each element and suggest that the core-level photoelectron spectra of Pd atoms in the interfacial layers and the inner layers of the Pd sandwich are split by ∼0.6 eV. The photoelectron spectra of the valence band show that the Pd sandwich retains the high density of states at the Fermi energy that is characteristic of Pd metal.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/sia.740201107
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  • 10
    Electronic Resource
    Electronic Resource
    Structural effects of fluorine substitution in proteins (1991)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Computational Chemistry 12 (1991), S. 180-185 
    Details
    ISSN: 0192-8651
    Keywords: Computational Chemistry and Molecular Modeling ; Biochemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Computer Science
    Notes: The consequences of substitution of fluorine for the para hydrogen of a phenylalanine residue in ribonuclease-S were investigated by conformational energy calculations using the AMBER force field. Both the fluorine-containing protein and the corresponding nonfluorinated material were subjected to conformational adjustment through energy minimization and the minimum energy structures so defined were compared. Fluorine substitution leads to small alterations in many atomic positions in the protein, with adjustments at at sites more than 0.5 nm from the fluorine appearing to be somewhat larger than those within the immediate vicinity of the fluorine. Several atoms proximate to the fluorine atom were observed to move toward the fluorine while others in the same vicinity move away. The greater bulk of the fluorine atom and the strongly different electronic properties of fluorine compared to hydrogen thus appear to be insufficient to cause a consistent, unidirectional change in nearest-neighbor interactions upon introduction of a fluorine atom into a protein structure. Virtually all changes in atomic positions that are predicted by these calculations would be barely detectable by a crystallographic study with a resolution of 0.2 nm.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcc.540120207
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