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  • 1990-1994  (1)
  • 1985-1989  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 32 (1985), S. 0 
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The regeneration (RG) of the oral apparatus (OA) by Climacostomum virens (Ciliophora, Heterotrichida) is examined by estimation of the ability of live cells to ingest food as well as by Nomarski interference contrast microscopy, bright field microscopy of protargol-stained specimens, and by scanning electron microscopy. When placed in a 6% (w/v) urea solution for ∼ 2 min 10 sec, populations of 10,000–100,000 cells shed a large part of their OA. In more than 90% of the cells that shed, the discarded segment is comprised of the apical membranelles, most of the adoral membranelles, and of a variable part of the buccal tube. After washing and incubation at 26°C, 50% of the cells regenerate a functional OA in 4 h 47 min, and after 5 h 26 min, 90% of the cells are able to ingest food. At any given moment during the process, 50–90% of the cells are morphologically in the same stage of RG.Seven stages (among which three are divided into two substages) of RG are defined. The process begins by the disorganization of the remnant oral structures. Concomitantly, kinetosomes multiply along the kineties of the zone of discontinuity and form the longitudinally oriented oral primordium. The latter gives rise to the adoral primordium, which rapidly produces the adoral zone of membranelles (AZM), and to the paroral primordium, which subsequently forms the apical membranelles, the buccal peristomial kineties, and the paroral kinety. Morphogenetic movements lead to incurvation of the AZM and the frontal field and to invagination of the buccal tube.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 22 (1992), S. 62-71 
    ISSN: 0886-1544
    Keywords: actin filaments ; actin isoforms ; anti-actin monoclonal antibodies ; cytoskeleton ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The anti-actin monoclonal antibody (mab) JLA20 (Lin: Proc. Natl. Acad. Sci. U.S.A. 78:2335-2339, 1981) labels a 43 kD protein on Western blots of Climacostomum cell extracts; this protein does not react with an anti-α-smooth muscle actin mab (Skalli et al.: J. Cell Biol. 103:2787-2796, 1986) nor with an anti-α-sarcomeric actin mab (Skalli et al.: Am. J. Pathol. 130:515-531, 1988). This protein binds to DNAse I and can be purified by DNAse I affinity chromatography. The affinity-purified actin also reacts with mab JLA20. Two-dimensional gel analysis reveals that Climacostomum actin focuses as three spots which are more basic than the mammalian actin isoforms. After addition of KC1, the affinity-purified actin polymerizes into filaments as shown by electron microscopy after negative staining. © 1992 Wiley-Liss, Inc.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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