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  • 1
    Electronic Resource
    Electronic Resource
    Secondary Force-Mediated Perturbations of Antifluorescein Monoclonal Antibodies 4-4-20 and 9-40 as Determined by Circular Dichroism (1998)
    Springer
    The protein journal 17 (1998), S. 237-244 
    Details
    ISSN: 1573-4943
    Keywords: Circular dichroism ; antibody secondary forces ; fluorescein ; monofluoresceinated peptides ; interfacial protein chemistry ; antibody dynamics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Secondary forces have been defined as those interactions between antibody and antigen that occur external to the antibody active site. Previous investigations indicated that non-active-site secondary interactions can modulate immune complex stability and may influence antibody variable domain conformation and/or dynamics. To assess secondary force-induced perturbations of monoclonal antibodies 4-4-20 and 9-40 a series of monofluoresceinated peptides was reacted and the various interactions analyzed by circular dichroism (CD). The mAbs 4-4-20 and 9-40 vary by nearly 1000-fold in their respective affinities for the fluorescein ligand, yet both immunoglobulins are highly related at the primary structural (idiotype) level. Near-UV CD spectra were evaluated as well as the induced optical activity (visible CD) of the antibody-bound fluorescein moiety when covalently attached to various peptide carriers. Comparative spectral studies revealed significant differences in the near-UV CD spectra of mAbs 9-40 and 4-4-20 relative to the various peptide antigens and to one another. CD spectra were interpreted as reflecting differential secondary force-induced perturbations of the antibody variable domains as well as intrinsic differences between the two mAbs.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1022532618038
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  • 2
    Electronic Resource
    Electronic Resource
    Intracellular vesicle movement, cAMP and myosin II in Dictyostelium (1990)
    Chichester [u.a.] : Wiley-Blackwell
    Developmental Genetics 11 (1990), S. 341-353 
    Details
    ISSN: 0192-253X
    Keywords: Vesicle movement ; myosin II ; cAMP ; Dictyostelium ; actin ; computer-assisted motion analysis ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Dictyostelium amoebae were analyzed before and after rapid addition of 10-6 M cAMP for cellular motility, dynamic shape changes, and intracellular particle movement. Before cAMP addition, amoebae moved in a persistent anterior fashion and were elongate with F-actin localized predominantly in the anterior pseudopod. Intracellular particles moved rapidly and anteriorly. Within seconds after 10-6 M cAMP addition, cells stopped translocating, pseudopod formation ceased, intra-cellular particle movement was depressed, and F-actin was lost from the pseudopod and concomitantly relocalized in the cell cortex After 10 seconds, expansion zones reappeared but were small and no longer anteriorly localized. Vesicle movement partially rebounded but was no longer anteriorly directed. The myosin II null mutant HS2215 exhibited both depressed cellular translocation and vesicle movement. The addition of cAMP to HS2215 cells did not result in any detectable change in the random, depressed movement of particles. The results with HS2215 suggest that myosin II is essential for (1) rapid cellular translocation, (2) cellular polarity, (3) rapid particle movement, (4) anteriorly directed particle movement, and (5) the cAMP response. Electron micrographs suggest that at least half of the particles examined in this study contain in turn smaller membrane bound vesicles or multilameilar membrane bodies. The possible role of these vesicles is discussed.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/dvg.1020110505
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