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  • Biochemistry and Biotechnology  (5)
  • High resolution GC-MS
  • Wiley-Blackwell  (5)
  • 1990-1994  (5)
  • 1
    Electronic Resource
    Electronic Resource
    Stabilization of substilisin E in organic solvents by site-directed mutagenesis (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 39 (1992), S. 141-147 
    Details
    ISSN: 0006-3592
    Keywords: protein engineering ; enzymes in organic solvents ; protein stabilization ; subtilisin E ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Subtilisin E was rationally engineered to improve its stability in polar organic solvents such as dimethylformamide (DMF). A charged surface residue, Asp248, was substituted by three amino acids of increasing hydrophobicity, Asn, Ala, and Leu; all three variants were stabilized with respect to wild type in 80% DMF. This stabilization was only observed in the presence of high concentrations of the organic solvent: no stability enhancements were observed in 40% DMF. In contrast, the mutation Asn218 → Ser alters internal hydrogen bonding interactions and stabilizes subtilisin E in both 40% and 80% DMF. This study provides additional evidence that substitution of surface-charged residues is a generally useful mechanism for stabilizing enzymes in organic media and that the stabilizing effects of such substitutions are unique to highly altered solvent environments. The effects of the single amino acid substitutions on free energies of stabilization are additive in the Asp248 → Asn + Asn218 → Ser combination variant, yielding an enzyme that is 3.4 times more stable than wild type in 80% DMF.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260390204
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  • 2
    Electronic Resource
    Electronic Resource
    Enhanced release of rosmarinic acid from Coleus blumei permeabilized by dimethyl sulfoxide (DMSO) while preserving cell viability and growth (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 40 (1992), S. 459-464 
    Details
    ISSN: 0006-3592
    Keywords: permeabilization ; dimethyl sulfoxide ; Coleus blumei ; preconditioning ; cell viability ; rosmarinic acid ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Continuous permeabilization of preconditioned Coleus blumei cells with dimethyl sulfoxide (DMSO) is shown to be an effective strategy for the enhanced release of rosmarinic acid (RA) while preserving cell viability. When nonpreconditioned cells were permeabilized with DMSO, they lost their viability at DMSO concentrations higher than a critical value located between 0.1% and 0.5% DMSO. Product release was low [0.49 g RA/100 g dry cell weight (DCW)] at 0.1% DMSO. Preconditioning cells at 0.1% DMSO ensured high viability at DMSO concentrations of 0.5%, 1.0%, and 1.5%. Product release reached a maximum of 2.85 g RA/100 g DCW at 0.5% DMSO, which was 66.4% of the total rosmarinic acid produced. © 1992 John Wiley & Sons, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260400403
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  • 3
    Electronic Resource
    Electronic Resource
    Extracellular calcium modulates proliferation of factor dependent hemopoietic cells (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Cell Biochemistry and Function 11 (1993), S. 101-105 
    Details
    ISSN: 0263-6484
    Keywords: Calcium ; cell proliferation ; calcium blockers ; FDCP-1 cells ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Blockade of the calcium channel inhibited, in a dose-dependent manner, the proliferation of the IL-3 dependent FDCP-1 cell line and normal murine bone marrow cells. Similar results were obtained by lowering the amount of extracellular calcium using specific chelators or a calcium-free medium. These results suggest that factor-dependent cell proliferation is highly sensitive to fluctuations in the concentration of extracellular calcium.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cbf.290110205
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  • 4
    Electronic Resource
    Electronic Resource
    Characterization of the acute phase serum protein response in pigs (1994)
    Weinheim : Wiley-Blackwell
    Electrophoresis 15 (1994), S. 672-676 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Acute inflammation was induced in pigs using a single subcutaneous turpentine injection. The acute phase serum protein response was analyzed using crossed immunoelectrophoresis and immunodiffusion. The concentration of C reactive protein and haptoglobin increases 5-7 times 48 h after the injection, whereas the concentration of an α2-globulin, named pig major acute phase protein (pig-MAP), increases at least 15-fold. A molecular mass of 115 kDa for pig-MAP was determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. This protein did not crossreact with antisera to human hemopexin, ceruloplasmin, H-kininogen and complement factor C3. Albumin and α-lipoprotein were negative acute phase proteins because their concentration significantly decreased during inflammation. Finally, the concentration of α1-acid glycoprotein, fetuin, α1-protease inhibitor, transferrin and α2-macro-globulins, as well as total proteins, did not change significantly during inflammation.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150150195
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  • 5
    Electronic Resource
    Electronic Resource
    Protein blot assays specific for the discrimination of the centromere autoantigen, CENP-A, from human cells (1993)
    Weinheim : Wiley-Blackwell
    Electrophoresis 14 (1993), S. 909-916 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The Western or protein blot has proven to be a valuable resource in detecting discrete, immunoreactive antigen targets associated with a variety of autoimmune diseases. As the roster of autoantigens has expanded, it has become increasingly common to tailor specific gel or blot conditions to a particular polypeptide antigen. Two such assays are reported here as applied to the fractionation and visualization of human centromere protein (CENP-A), a centromere autoantigen associated with the rheumatic disease, systemic sclerosis. The centromere antigens are effectively solubilized in the presence of 1 M MgCl2 to allow for further purification. CENP-A copurifies with the histone proteins, primarily H3 and H4. The two CENP-A-specific protein blot assays separate CENP-A from the histone proteins and enhance CENP-A immuno-reactivity. The first assay is based on the use of acid-urea gels with a Triton X-100 concentration chosen to maximize separation of CENP-A from all the histones. The second assay is based on sodium dodecyl sulfate-polyacrylamide gel electrophoresis to differentiate two very basic proteins of similar molecular weight, namely CENP-A and histone H3. For each gel system, a selective choice of associated immunoblot parameters allows for the reproducible discrimination of the CENP-A antigen.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.11501401145
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