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  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Gene Structure and Expression 1216 (1993), S. 431-440 
    ISSN: 0167-4781
    Keywords: (Mouse) ; Baculovirus expression vector ; Histidine decarboxylase ; Mastocytoma cell ; Post-translational processing
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0167-4889
    Keywords: 12-O-Tetradecanoylphorbol-13-acetate ; Dexamethasone ; Histidine decarboxylase ; Histidine decarboxylase mRNA
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Molecular Cell Research 1133 (1992), S. 179-186 
    ISSN: 0167-4889
    Keywords: Calcium ; Histidine decarboxylase ; Histidine decarboxylase mRNA ; cyclic AMP
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 0014-5793
    Keywords: Amino acid sequence ; Dopa decarboxylase ; Histidine decarboxylase ; Mastocytoma P-815 cell ; Polymerase chain reaction ; cDNA sequence
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Molecular Cell Research 928 (1987), S. 227-234 
    ISSN: 0167-4889
    Keywords: (Mastocytoma P-815 cell) ; Dexamethasone ; Enzyme induction ; Histidine decarboxylase
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 22 (1976), S. 539-549 
    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 concept of the optimal synthesis of dynamic process systems with uncertain parameters is introduced. A structure parameter approach is used to theoretically derive the necessary condition for the optimal performance system structure, and an effective algorithm for implementing the synthesis method is presented. The results are applied to the optimal synthesis of a reactor-separator system for the dynamic start-up of two reaction systems.
    Additional Material: 8 Ill.
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  • 7
    ISSN: 0001-1541
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Unpredictable variations in the values of plant parameters around their nominal values are often encountered in actual operation of process plants. In order to assure that process performance meets specifications, it is preferable to design and control the process, taking into account the uncertainty in the values of the plant parameters. In this paper, a method to minimize the maximum decrease in the process performance caused by the hypothetical worst parameter variations is proposed. Necessary condition for the worst parameter variations is derived for a class of distributed parameter systems by means of the maximum principle, and then the method for obtaining the optimal design and control subject to the worst parameter variations are discussed. The method is applied to the design of a tubular reactor associated with catalyst activity decay. The reactor obtained is fairly insensitive to the variations in the process parameters while maintaining fairly good performance even at the nominal values of parameters.
    Additional Material: 10 Ill.
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  • 8
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 45 (1995), S. 304-309 
    ISSN: 0006-3592
    Keywords: phenol ; substituted phenol ; tyrosinase ; immobilization ; chitosan ; coagulant ; immobilized enzyme ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Removal of phenols and aromatic amines from industrial wastewater by tyrosinase was investigated. A color change from colorless to darkbrown was observed, but no precipitate was formed. Colored products were found to be easily removed by a combination treatment with tyrosinase and a cationic polymer coagulant containing amino group, such as hexamethylenediamine-epichlorohidrin polycondensate, polyethleneimine, or chitosan. The first two coagulants, synthetic polymers, were more effective than chitosan, a polymer produced in crustacean shells. Phenols and aromatic amines are not precipitated by any kind of coagulants, but their enzymatic reaction products are easily precipitated by a cationic polymer coagulant. These results indicate that the combination of tyrosinase and a cationic polymer coagulant is effective in removing carcinogenic phenols and aromatic amines from an aqueous solution. Immobilization of tyrosinase on magnetite gave a good retention of activity (80%) and storage stability i.e., only 5% loss after 15 days of storage at ambient temperature. In the treatment of immobilized tyrosinase, colored enzymatic reaction products were removed by less coagulant compared with soluble tyrosinase. © 1995 John Wiley & Sons, Inc.
    Additional Material: 9 Ill.
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  • 9
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 51 (1996), S. 126-130 
    ISSN: 0006-3592
    Keywords: chlorophenol ; peroxidase ; immobilization ; magnetite ; immobilized enzyme ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Immobilization of horseradish peroxidase on magnetite and removal of chlorophenols using immobilized enzyme were investigated. Immobilization by physical adsorption on magnetite was much more effective than that by the crosslinking method, and the enzyme was found to be immobilized at 100% of retained activity. In addition, it was discovered that horseradish peroxidase was selectively adsorbed on magnetite, and the immobilization resulted in a 20-fold purification rate for crude enzyme. When immobilized peroxidase was used to treat a solution containing various chlorophenols, p-chlorophenol, 2,4-dichlorophenol, 2,4,5-trichlorophenol, 2,4,6-trichlorophenol, 2,3,4,6-tetrachlorophenol, and pentachlorophenol, each chlorophenol was almost 100% removed, and also the removal of total organic carbon (TOC) and adsorbable organic halogen (AOX) reached more than 90%, respectively. However, in the case of soluble peroxidase, complete removal of each chlorophenol could not be attained, and in particular, the removal of 2,4,5-trichlorophenol was the lowest, with a removal rate of only 36%. © 1996 John Wiley & Sons, Inc.
    Additional Material: 4 Ill.
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  • 10
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 39 (1992), S. 20-26 
    ISSN: 0006-3592
    Keywords: reversed micelle ; extraction ; solubilizing water ; AOT ; protein ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The extraction of protein using reversed micelles was investigated in relation to the amount of solubilizing water in the reversed micellar organic phase. The minimal concentration of amphiphilic molecule di-2-ethylhexyl sodium sulfosuccinate (C20H37O7Na) (AOT) required for 100% cytochrome c extraction was recognized. This critical AOT concentration increased with protein concentration in the aqueous phase. On this minimal AOT condition, the molar ratio of solubilizing water to extracted protein was found to be a constant of 3500 under CKCI = 1.0 × 102 mol · m-3 in this system. This ratio means the hydrophillic surroundings required for extracting one protein molecule into the micellar organic phase under the suitable pH and salt concentration for the forward extraction. In this regard, AOT molecules seemed to take the part of water solubilizing agent in the reversed micellar extraction. This role of AOT is important to extract protein under the suitable pH and salt concentration. The amount of solubilizing water in the protein-containing system was larger than in the protein-free system. This difference shows that the water molecules accompany the extracted protein into the reversed micellar organic phase at constant ratio 2200 under CKCI = 1.0 × 102 mol · m-3, i.e., accompanying water molecules per one extracted protein. The minimal AOT concentration increased with ionic strength. On this minimal AOT condition, the molar ratio of solubilizing water to extracted protein also increased with ionic strength, so that in higher ionic strength, more solubilizing water was required. Then more AOT was required to provide the hydrophillic surroundings for protein. The pH affected the minimal AOT concentration required for 100% protein extraction.
    Additional Material: 9 Ill.
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