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  • 1
    Electronic Resource
    Electronic Resource
    Studien über das Indium (1910)
    Weinheim : Wiley-Blackwell
    Zeitschrift für anorganische Chemie 66 (1910), S. 288-321 
    Details
    ISSN: 0863-1778
    Keywords: Chemistry ; Inorganic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Indium lässt sich durch Fällung des Hydroxyds mit Ammoniak und Erhitzen auf 850° im Filtertiegel mit großer Genauigkeit quantitativ bestimmen.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/zaac.19100660119
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Adsorptionsuntersuchungen an Organokieselsäurepolymeren (1992)
    Weinheim : Wiley-Blackwell
    Zeitschrift für anorganische Chemie 612 (1992), S. 137-142 
    Details
    ISSN: 0044-2313
    Keywords: Adsorption and swelling ; isothermes ; specific surfaces ; organosilicic acid ; double four-ring silicate units ; Chemistry ; Inorganic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: Adsorption Studies on Organosilic Acid PolymersWe present four organosilic acid polymers containing double-4-ring silicate units cross-linked at different degree by different organosilicon bridges. BET surfaces were determined and adsorption isotherms of n-hexane, benzene, nitrogen and water were measured. All polymers are hydrophobic, one of them behaves microporously, the other are unporous. With organic adsorptives, swelling and adsorption occur simultaneously. Possible relations of microporosity and structure are discussed.
    Notes: BET-Oberflächen und Isothermen von n-Hexan, Benzen, Wasser und Stickstoff wurden an vier Organokieselsäurepolymeren vermessen, die sich im Vernetzungsgrad der Doppelvierring-Kieselsäureeinheiten Si8O20 und in der Struktur der Brücken unterscheiden. Ein Polymere ist mikroporös, die anderen sind unporös. Alle Polymere verhalten sich hydrophob. Neben der Adsorption tritt Quellung bei der Einwirkung organischer Adsorptive auf. Die Zusammenhänge zwischen der Länge der Brücken und der Porosität werden diskutiert.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/zaac.19926120123
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Gewinnung und Charakterisierung von Prolidase aus Escherichia coli B, II. Charakterisierung, Reinigung und Trägerfixierung des Enzyms (1982)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 2 (1982), S. 161-170 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Prolidase, a specific exopeptidase, is isolated from Escherichia coli B. The enzyme being present in the raw extract is purified and enriched by fractionated ammonium sulfate precipitation, ion exchange chromatography on DEAE-Sephadex A 50 as well as by gel filtration on Sepharose 4 B. Total yield of prolidase amounts to 19% with a 67fold enrichmentSubstrate specifity of the enzyme mainly corresponds to that of the animal prolidase. It is able to hydrolize the imido linkage at the N-terminal end of prolin in the case of di- and tripeptides. The temperature optimum of prolidase from E. coli B is 37 °C, the pH-optimum from pH 7.6 to 9.0. Storage stability at pH 8.6 and a temperature of 4 °C is optimal. The enzyme is only active in presence of Mn2+-ions. This metal cannot be replaced by Mg2-- or Zn2+-ionsA high enzyme activity and storage stability in presence of Mn2+-ions can be reached by immobilization of the prolidase, by covalent binding on Sepharose 6 B, adsorption on DEAE-Sephadex as well as by combination with glutar dialdehyde on DEAE-Sephadex.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370020208
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Continuous production of protein hydrolysates in immobilized enzyme reactors (1987)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 7 (1987), S. 227-235 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: The digestion of several proteins, casein, α-lactalbumin, human serum albumin and a mixture of whey proteins by immobilized pronase, thermitase and leucine aminopeptidase was studied on various conditions in five types of enzyme reactors. Reactors and operating conditions were designed to maximize the extent of hydrolysis and to minimize the adverse effects of the macromolecular nature of the substrates. A simple analytical method was developed to follow routinely the extent of hydrolysis. Substrate proteins were subjected to various pretreatments intended to disturb their native structure. The maximum feasible extent of hydrolysis in the reactor effluent, which is an average quantity, clustered around the magic figure of 33% in all systems studied. Protein digestion in bubbled column reactors charged with the polyaminomethylstyrene-fixed thermostable proteinase “thermitase” and operated at 50 to 60°C turned out to be the most efficient setup to produce continuously amino acid/peptide mixtures.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370070307
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    Paper (German National Licenses)
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