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  • Polymer and Materials Science  (2)
  • 1
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 22 (1983), S. 465-473 
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Activation of mutant β-galactosidase by antibodies can be explained by a “selection” mechanism in which the antibody binds and stabilizes those mutants in a native-like conformation and by an “induction” mechanism where binding of the antibody itself induces a conformational change activating β-galactosidase. The “selection” hypothesis was tested by passing β-galactosidase through a column packed with monoclonal antibody-derivatized Sepharose. The antibody retains the active, in preference to the inactive, proteins. The “induction” mechanism was tested by mixing antibody-Sepharose with mutant β-galactosidase and measuring enzyme activity before mixing and that remaining in the supernatant. The activity of the antibody-Sepharose pellet exceeded the sum of the original activity plus supernatant activity. As a result of these experiments, both mechanisms are found to be operative.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: In aqueous solution, melittin structure, investigated by CD and 1H-nmr, depends on pH and ionic composition, which also regulate the aggregation state of the peptide. When interacting with phospholipids, however, melittin exhibits a right-handed helical conformation without any evidence of oligomeric association. The overall bilayer structure of phospholipid aqueous dispersions is also maintained in the presence of melittin, although the permeability to aqueous solutes is considerably increased. Small-angle neutron-diffraction analysis of oriented multilayers confirms the existence of a lamellar profile, despite the presence of the peptide throughout each bilayer and exchangeable protons almost reaching the center of the hydrophobic alkyl chains region.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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