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  • 1
    Electronic Resource
    Electronic Resource
    Method to identify hexahistidine fusion proteins in crude cellular lysate (1994)
    Springer
    Biotechnology techniques 8 (1994), S. 39-44 
    Details
    ISSN: 1573-6784
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary The strong interaction of chelated nickel ions with a hexahistidine peptide was utilized to identify hexahistidine fusion proteins in crude cellular lysates. The technique involves a Ni2+-nitrilotriacetic acid derivative labelled with alkaline phosphatase. The new reagent was used to probe for hexahistidine fusion proteins after SDS-PAGE electrophoresis and blotting onto nitrocellulose. The minimal amount of fusion protein which could be detected with this method was 0.1 μg.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00207631
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  • 2
    Electronic Resource
    Electronic Resource
    Reinigung der D-Oxynitrilase aus Mandeln mit Hilfe der Affinitäts-Chromatographie (1983)
    New York, NY : Wiley-Blackwell
    Helvetica Chimica Acta 66 (1983), S. 489-493 
    Details
    ISSN: 0018-019X
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A Rapid Purification of D-Oxynitrilase from Almond Meal by Affinity ChromatographyOxynitrilase from almond meal is capable of catalyzing the stereospecific addition of cyanide to a variety of aldehydes. Thus, the enzyme is potentially useful in the synthesis of optically active cyanohydrins on a preparative scale [1]. As the currently available purification procedures for this enzyme [2] are rather tedious, we have elaborated a simple and rapid procedure based on affinity chromatography. An inhibitor for the enzyme, methyl p-(3-aminopropoxy)benzoate (4), has been synthesized and attached covalently to Sepharose 4B as a solid matrix (5). With this affinity gel it was possible to prepare the D-oxynitrilase in a simple procedure with high yields.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/hlca.19830660210
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  • 3
    Electronic Resource
    Electronic Resource
    Enantionselektive Synthese des L-Threonins (1987)
    New York, NY : Wiley-Blackwell
    Helvetica Chimica Acta 70 (1987), S. 232-236 
    Details
    ISSN: 0018-019X
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: An Enantionselective Synthesis of L-ThreonineAn enantioselective synthesis of L-threonine (1) is described. Racemic ethyl 2-acetamido-3-oxobutyrate (6) was synthesized from ethyl acetoacetate (2) [4][5] and then transformed to the epimeric optically active alcohols 7a and 7b by microbiological reduction with Saccharomyces rouxii. The Mixture 7a/7b could be converted to 1 by slightly modified, known Methods in a yield of ca. 52% with respect to 7a/7b.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/hlca.19870700128
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  • 4
    Electronic Resource
    Electronic Resource
    Immobilization of β-galactosidase for application in organic chemistry using a chelating peptide (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 42 (1993), S. 178-184 
    Details
    ISSN: 0006-3592
    Keywords: recombinant β-galactosidase fusion protein ; chelating peptide ; immobilized metal affinity chromatography ; immobilized enzyme ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The strong interaction of hexa-histidine fusion proteins with metal chelate adsorbents was utilized to immobilize β-galactosidase with a hexa-histidine peptide at the N-terminus to the Ni2+-nitrilotriacetic acid adsorbent. The fusion protein was cloned and expressed in Escherichia coli. The purified soluble fusion protein showed the same specific activity as the purified β-galactosidase and retained 64 percent of its β-galactosidase activity when bound to the adsorbent. To demonstrate the potential of the immobilized β-galactosidase in organic chemistry, allyl-β-D-galactosidase was synthesized from lactose and allyl alcohol on a gram scale. The same enzyme preparation was reused in three subsequent batches to prepare the model compound with high yield. © 1993 John Wiley & Sons, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260420205
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