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  • Biochemistry and Biotechnology  (2)
  • Wiley-Blackwell  (2)
  • American Association for the Advancement of Science (AAAS)
  • 1985-1989  (1)
  • 1970-1974  (1)
Collection
Keywords
Publisher
  • Wiley-Blackwell  (2)
  • American Association for the Advancement of Science (AAAS)
Years
Year
  • 1
    Electronic Resource
    Electronic Resource
    Kinetics of protein release from yeast sonicated in batch and flow systems at 20 kHz (1972)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 14 (1972), S. 33-42 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The release constant, k, of brewers yeast sonicated at powers up to 200 W at 20 kHz has been shown to be independent of cell concentration up to values of 60 g made up to 100 ml. It is inversely proportional to the volume of the treatment vessel in the range 75 to 450 ml, and almost proportional to the input acoustic power from 60 to 195 acoustic watts. A flow system is described and a relationship linking protein release, flow rate, and the protein release constant, determined from batch experiments, is derived. Good agreement between the theoretical prediction of protein release and experimental results with the flow system was obtained.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260140105
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Characterization of human skin fibroblast extracellular proteins by two-dimensional polyacrylamide gel electrophoresis (1988)
    Weinheim : Wiley-Blackwell
    Electrophoresis 9 (1988), S. 343-351 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Human skin fibroblasts secrete over 50 proteins into the culture medium. In this paper these are characterised using two-dimensional polyacrylamide gel electrophoresis and peptide mapping of proteins metabolically labelled in the presence and absence of tunicamycin. Thirty of these proteins have been shown to be N-glycosides, 4 are O-glycosides and 10 are not glycosylated. Of the major proteins, groups 1-4 have previously been shown to be fibroblast specific. Peptide mapping and tunicamycin treatment has identified that groups 1 and 2, and 3 and 4 are closely related and that groups 1 and 3 arise by N-glycosylation of 2 and 4, respectively. The unglycosylated precursor forms of several other proteins have also been identified. This approach to the analysis of protein secretion provides an abundance of information on many proteins simultaneously and can be used to assess the changes in protein secretion associated with development, and to identify extracellular growth factors and other regulatory proteins.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150090711
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    Paper (German National Licenses)
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