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  • 1
    Electronic Resource
    Electronic Resource
    The concentration of protein solutions by normal freezing (1974)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 16 (1974), S. 21-39 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: An apparatus is described which is designed for preparative freeze concentration experiments by the technique of normal freezing. It has a capacity of approximately 22 liters distributed over twelve vessels. The influence of various geometrical and chemical parameters such as stirring speed, crystallization rate, and sample composition on the normal freezing of protein solutions are discussed. For dilute protein solutions (〈0.1%) the concentration factor generally was 8- to 10-fold with recoveries of 90-100 percent. With higher protein concentrations and at ionic strengths higher than approximately 0.05, the recovery was decreased. No loss of activity was detected when concentrating enzyme solutions.
    Additional Material: 14 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260160104
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Large-scale preparation of a lectin from sunn hemp seeds (Crotalaria juncea) (1980)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 22 (1980), S. 79-88 
    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 procedure for large-scale preparation of a lectin from Crotalaria juncea seeds is described. The method involve fractionation by pH- and ammonium sulfate precipitation followed by biospecific affinity chromatography. The adsorbent used for the affinity chromatography was prepared by coupling galactose to Sepharose 6B activated with divinylsulfone. A comparison of different apparatus and techniques involved in the preparation is discussed. The yield and quality of the lectin prepared at a large scale were comparable with laboratory-scale preparation. From 50 kg Crotalaria juncea beans, 14.4 g Crotalaria lectin were obtained.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260220107
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Use of immobilized metal ions as a negative adsorbent for purification of enzymes: Application to phosphoglycerate mutase from chicken muscle extract and horseradish peroxidase (1992)
    New York, NY : Wiley-Blackwell
    Biomedical Chromatography 6 (1992), S. 172-176 
    Details
    ISSN: 0269-3879
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Two enzymes, phosphoglycerate mutase and peroxidase, were purified by using an immobilized metal ion adsorbent for the removal of unwanted proteins. The mutase was obtained pure from a single column, whereas the purification of peroxidase required the use of a thiophilic adsorbent in a tandem. The capacity was 2.5 mg pure peroxidase per mL gel.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bmc.1130060404
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    Paper (German National Licenses)
    Fulltext
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