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  • 1980-1984  (6)
  • 1
    Electronic Resource
    Electronic Resource
    Production and Textural Properties of Soy-Cheese Whey Curd (1983)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 48 (1983), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Soy-cheese whey curd was prepared by mixing soymilk and cheese whey with the addition of glucono-delta-lactone (GDL) to coagulate the proteins. Three soymilk concentrations, 6:1, 8:1 and 10:1 (water:bean, v/w), and four cheese whey levels, 3%, 4.5%, 5.25% and 6% (w/v), were used. Heating the GDL treated soy-cheese whey milk in a hot water bath at 85°C for 25 min consistently produced a smooth and compact. curd without syneresis. Textural properties of the curd were tested by an Instron machine. Five parameters-stiffness, bioyield point, firmness, relaxation and plasticity—were determined. Among these, only stiffness and firmness could be used as the textural parameters for the curd.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1983.tb03540.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Monoclonal Antibodies to Gel-Excised Glial Filament Protein and Their Reactivities with Other Intermediate Filament Proteins (1984)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 42 (1984), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: A series of 14 monoclonal antibodies (MAs) has been obtained from a single rat-mouse fusion using gel-excised bovine glial filament (GF) proteins as immunogens. These MAs were characterized by two separate immunochemical assays and by two different immunohistochemical methods. Nine MAs demonstrated specificity for GF proteins. One MA also recognized an epitope shared by intermediate filaments (IF) of the vimentin class (VF). Using the enzyme-linked immunosorbent assay, four of the MAs recognized 200,000, 150,000, and 51,000 dalton proteins, suggesting that these MAs were specific for GF proteins (the 51,000 dalton protein) and neurofilament (NF) proteins (the two high-molecular-weight proteins). However, in both of the immunohistochemical assay systems, these MAs stained neurons and their processes but not astroglial cells. These observations strongly suggest that the 51,000–dalton protein recognized by these four MAs was not derived from GF proteins but instead represents derivatives of NF protein subunits comigrating in gels with GF proteins. These data provide additional information concerning the unique and shared antigenic determinants of the three classes of IF (NF, GF, and VF) of the CNS. In addition, they draw attention to the fact that proteins of certain IF may undergo degradation and comigrate in gels with the proteins of unrelated IF. This emphasizes the need for the use of independent immunochemical and immunohistochemical assays in the characterization of the specificity of MAs.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1984.tb09692.x
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Preparative Separation and Amino Acid Composition of Neurofilament Triplet Proteins (1982)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 38 (1982), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Intact neurofilaments were isolated from bovine spinal cord white matter, washed by sedimentation in 0.1 m-NaCl, and extracted with 8 m-urea. Solubilized neurofilament triplet proteins of molecular weights approximately 68,000 (P68), 150,000 (P150), and 200,000 (P200) were purified by preparative electrophoresis, using an LKB 7900 Uniphor apparatus. The method provides for an enhanced yield of purified protein and has markedly reduced admixture of electrophoresed protein with acrylamide and associated protein contaminants. Amino acid compositions of the purified neurofilament triplet proteins are reported and compared.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1982.tb10861.x
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Proteins of the Outer Membrane of Gram-Negative Bacteria (1980)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Microbiology 34 (1980), S. 369-422 
    Details
    ISSN: 0066-4227
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.mi.34.100180.002101
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    On compact kähler manifolds of nonnegative bisectional curvature, I (1981)
    Springer
    Acta mathematica 147 (1981), S. 51-56 
    Details
    ISSN: 1871-2509
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mathematics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02392867
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    Paper (German National Licenses)
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  • 6
    Electronic Resource
    Electronic Resource
    On compact Kähler manifolds of nonnegative bisectional curvature, II (1981)
    Springer
    Acta mathematica 147 (1981), S. 57-70 
    Details
    ISSN: 1871-2509
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mathematics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02392868
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    Paper (German National Licenses)
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