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  • motility  (3)
  • 01180938; AESOPS; Antarctic Environments Southern Ocean Process Study; Biogenic silica; Bottle, Niskin; Bottle number; DEPTH, water; Dissolution of biogenic silica, specific; Irradiance; JGOFS; Joint Global Ocean Flux Study; KIWI-8; KIWI-8/4-9; NIS; Production of biogenic silica; Roger A. Revelle; Silicate; Southern Ocean  (1)
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  • 1
    Digitale Medien
    Digitale Medien
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 24 (1993), S. 17-28 
    ISSN: 0886-1544
    Schlagwort(e): antibody ; motility ; axoneme ; ATPase ; Life and Medical Sciences ; Cell & Developmental Biology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Medizin
    Notizen: Three forms of dynein (22S, 19S, and 12S) were purified from Paramecium cilia. Two classes of monoclonal antibodies against purified 22S dynein were generated. One class reacted on immunoblots with the heavy chains of 22S, 19S, and 12S dyneins; the second class reacted with an 88 kD intermediate chain of 22S dynein. Polyclonal antiserum to the heavy chains of 22S dynein reacted with the γ-heavy chain of 22S and 19S dyneins. A previously described antiserum raised against 22S dynein [Travis et al.: Biochim. Biophys. Acta 966:73-83, 1988] recognized the γ-heavy chain of 22S dynein which was also present in 19S and 12S dyneins, along with the 88 and 76 kD intermediate chains of 22S dynein. This antiserum was also able to immunoprecipitate dynein from crude extracts of cilia.Electron microscopy revealed that the 22S dynein consisted mainly of two-headed particles with some three-headed particles present. The 12S dynein was mainly one-headed particles. The 19S dynein was a mixture of three-, two-, and one-headed particles. The immunological and electron microscopic studies showed that 19S dynein arises from 22S dynein, and that 12S dynein is heterogeneous, composed of the γ-heavy chain of 22S dynein and a unique dynein ATPase.The polyclonal antibodies were also used to detect cross-reactive proteins in other organisms. Both the anti-heavy chain and the anti-22S dynein sera reacted strongly with 22S outer arm dynein of Tetrahymena, but not with the 14S dynein of this organism. © 1993 Wiley-Liss, Inc.
    Zusätzliches Material: 8 Ill.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 30 (1995), S. 252-260 
    ISSN: 0886-1544
    Schlagwort(e): axoneme ; ciliary regulation ; cyclic nucleotides ; motility ; Life and Medical Sciences ; Cell & Developmental Biology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Medizin
    Notizen: In the ciliated protozoan Paramecium, swimming direction is regulated by voltage-gated Ca2+ channels in the ciliary membrane. In response to depolarizing stimuli, intraciliary Ca2+ rises, triggering reversal of the ciliary power stroke and backward swimming. One class of Ca2+ -unresponsive behavioral mutants of Paramecium, atalanta mutants, cannot swim backward even though they have functional Ca2+ channels in their ciliary membrane. Several atalanta mutants were characterized with regard to several Ca2+ -dependent activities, but no significant difference between wild type and the mutants was detected. However, one allelic group, atalanta A (initially characterized by Hinrichsen and Kung [1984: Genet. Res. Camb. 43:11-20]), showed a helical swimming path of opposite handedness from that of wild-type cells when detergent-permeabilized cells (“models”) were reactivated with MgATP. When cGMP-dependent protein kinase purified from wild-type cells was added to atalanta A models, the handedness of the swimming path was reversed. Cyclic GMP stimulated in vitro phosphorylation of several proteins in isolated cilia, and the pattern of phosphoproteins was very similar for wild type and atalanta mutants, with one exception: a protein of 59 kDa was phosphorylated much less in the mutant ata A. When ciliary proteins were separated by gel electrophoresis and then phosphorylated “on blot” by purified cGMP-dependent protein kinase, phosphoprotein patterns were similar in wild type and ata mutants except that a 48 kDa protein (p48) from ata A3 was more heavily phosphorylated. This difference in p48 phosphorylation was also observed with cGMP-dependent protein kinase purified from ata A3 mutant cells. Ciliary p48 may be part of the mechanism that regulates the orientation of the ciliary power stroke. © 1995 Wiley-Liss, Inc.
    Zusätzliches Material: 5 Ill.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 3
    Digitale Medien
    Digitale Medien
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 19 (1991), S. 91-98 
    ISSN: 0886-1544
    Schlagwort(e): motion analysis ; motility ; adaptation ; Life and Medical Sciences ; Cell & Developmental Biology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Medizin
    Notizen: Paramecium letraurelia is a ciliated protist that alters its swimming behavior in response to various stimuli. Like the sensory responses of many organisms, these responses in Paramecium show adaptation to continued stimulation. For quantitative studies of the initial response to stimulation. and of the time course of adaptation, we have developed a computerized motion analysis assay that can detect deviations from the normal swimming pattern in a population of cells. The motion of an average of ten cells was quantified during periods ranging from 15 to 60 seconds, with a time resolution of 1/15 seconds. During normal forward swimming, the maximum deviation from a straight-line path was less than 17°. Path deviations above this threshold value were defined as changes in swimming direction. The percentage of total path time that cells spent deviating from forward swimming was defined as percent directional changes (PDC). This parameter was used to construct dose-response curves for the behavioral effects of various externally added cations known to induce behavioral changes and also to show the time course of adaptation to a depolarizing K+ stimulus. This assay is a valuable tool for studies of chemoeffectors or mutations that alter the swimming behavior of Paramecium and may also be applicable to other motile organisms.
    Zusätzliches Material: 5 Ill.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 4
    Publikationsdatum: 2024-02-01
    Schlagwort(e): 01180938; AESOPS; Antarctic Environments Southern Ocean Process Study; Biogenic silica; Bottle, Niskin; Bottle number; DEPTH, water; Dissolution of biogenic silica, specific; Irradiance; JGOFS; Joint Global Ocean Flux Study; KIWI-8; KIWI-8/4-9; NIS; Production of biogenic silica; Roger A. Revelle; Silicate; Southern Ocean
    Materialart: Dataset
    Format: text/tab-separated-values, 48 data points
    Standort Signatur Erwartet Verfügbarkeit
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