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  • 1
    Electronic Resource
    Electronic Resource
    Proteolytic specificity of chicken cathepsin L on bovineβ-casein (1988)
    Springer
    Bioscience reports 8 (1988), S. 185-191 
    Details
    ISSN: 1573-4935
    Keywords: cathepsin L ; specificity ; β-casein ; proteolysis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The proteolytic specificity of chicken cathepsin L was studied using bovine β-casein as substrate. The peptide mixtures obtained after various times of hydrolysis were separated by RP-HPLC and ten peptides were identified. Chicken cathepsin L accepts proline residues in all positions except P 1 ′ . Looking at the amino acid residues on the amino side of the scissile bond we found three times the Tyr-Pro pair at P 1 ′ –P 2 ′ positions and that the S 1 ′ subsite can interact with modified amino acids such as phosphoserine.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01116463
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Binding of benzo(α)pyrene, ellipticine, and cis-parinaric acid to β-lactoglobulin: Influence of protein modifications (1992)
    Springer
    The protein journal 11 (1992), S. 645-652 
    Details
    ISSN: 1573-4943
    Keywords: β-lactoglobulin ; modifications ; ligand binding ; fluorescence ; dynamic light scattering
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The binding of benzo(α)pyrene, ellipticine, and cis-parinaric acid to native, esterified, and alkylated β-lactoglobulin was followed by enhancement of the ligand fluorescence. Three studied ligands bind to native or modified β-lactoglobulin in apparent molar ratios varying between 1/8 and 2/1, with apparent dissociation constants in the range of 10−8 M for ligand/β-lactoglobulin complexes. The studied, chemically modified β-lactoglobulin derivatives display higher binding affinities for all studied ligands, cis-parinaric acid excluded. The reductive alkylation of ε-NH2 lysyl residues of β-lactoglobulin increases the apparent molar ratios of benzo(α)pyrene and cis-parinaric acid, and decreases it for ellipticine. The esterified and native β-lactoglobulin complexed to the investigated ligands display similar stoichiometries. Dynamic light scattering study of ligand-β-lactoglobulin complexes in solution shows the formation of aggregates: the apparent hydrodynamic radius value of β-lactoglobulin dimer (3.4 nm) reaches 49, 46, and 74 nm upon addition and binding of benzo(α)pyrene, ellipticine, and cis-parinaric acid, respectively.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01024965
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  • 3
    Electronic Resource
    Electronic Resource
    Probing the fatty acid binding site of β-lactoglobulins (1993)
    Springer
    The protein journal 12 (1993), S. 443-449 
    Details
    ISSN: 1573-4943
    Keywords: Fatty acids ; binding site ; β-lactoglobulin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The interactions of fatty acids with porcine and bovine β-lactoglobulins were measured using tryptophan fluorescence enhancement. In the case of bovine β-lactoglobulin, the apparent binding constants for most of the saturated and unsaturated fatty acids were in the range of 10−7 M at neutralpH. Bovine β-lactoglobulin displays only one high affinity binding site for palmitate with an apparent dissociation constant of 1·10−7 M. The strength of the binding was decreasing in the following way: palmitate 〉 stearate 〉 myristate 〉 arachidate 〉 laurate. Caprylic and capric acids are not bound at all. The affinity of β-lactoglobulin for palmitate decreased as thepH of the incubation medium was lowered and BLG/palmitate complex was not observed atpH's lower than 4.5. Surprisingly, chemically modified bovine β-lactoglobulin and porcine β-lactoglobulin did not bind fatty acids in the applied conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01025044
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  • 4
    Electronic Resource
    Electronic Resource
    Conformation changes ofβ-lactoglobulin: An ATR infrared spectroscopic study of the effect ofpH and ethanol (1994)
    Springer
    The protein journal 13 (1994), S. 143-149 
    Details
    ISSN: 1573-4943
    Keywords: Β-Lactoglobulin ; structure ; sol-gel transition ; infrared ; principal component analysis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Fourier transform infrared spectroscopy has been applied to investigate the secondary structural changes ofΒ-lactoglobulin in water/ethanol mixtures. The studies were carried out at two differentpHs and at high protein concentrations. The spectra were recorded using an attenuated total reflection cell. The amide I band ofΒ-lactoglobulin in water reveals large amounts of intra extendedΒ-sheet structure. About 20% ethanol,Β-lactoglobulin unfolds andΒ-strand formation is observed.α-Helices are built up by increasing the ethanol concentration up to 30%. In 50% ethanol,Β-lactoglobulin gels providing the apparent pH are neutral. The secondary structural changes ofΒ-lactoglobulin were observed on the similarity maps obtained by Principal Component Analysis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01891973
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  • 5
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    Fluorescence Spectroscopy as a Promising Tool for a Polyphasic Approach to Pseudomonad Taxonomy (2008)
    Springer
    Details
    Publication Date: 2008-09-25
    Print ISSN: 0343-8651
    Electronic ISSN: 1432-0991
    Topics: Biology , Medicine
    Published by Springer
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