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  • Life and Medical Sciences  (4)
  • 1985-1989  (4)
  • 1
    Electronic Resource
    Electronic Resource
    Contributions of the β-subunit to spectrin structure and function (1989)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 12 (1989), S. 248-263 
    Details
    ISSN: 0886-1544
    Keywords: ankyrin ; adducin ; protein 4.1 ; correlation length ; flexural rigidity ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The three avian spectrins that have been characterized consist of a common α-subunit (240 kD) paired with an isoform-specific β-subunit from either erythrocyte (220 or 230 kD), brain (235 kD), or intestinal brush border (260 kD). Analysis of avian spectrins, with their naturally occurring “subunit replacement” has proved useful in assessing the relative contribution of each subunit to spectrin function. In this study we have completed a survey of avian spectrin binding properties and present morphometric analysis of the relative flexibility and linearity of various avian and human spectrin isoforms. Evidence is presented that, like its mammalian counterpart, avian brain spectrin binds human erythroid ankyrin with low affinity. Cosedimentation analysis demonstrates that (1) avian erythroid protein 4.1 stimulates spectrin-actin binding of both mammalian and avian erythrocyte and brain spectrins, but not the TW 260/240 isoform, (2) calpactin I does not potentiate actin binding of either TW 260/240 or brain spectrin, and (3) erythrocyte adducin does not stimulate the interaction of TW 260/240 with actin.In addition, a morphometric analysis of rotary-shadow images of spectrin isoforms, individual subunits, and reconstituted complexes from isolated subunits was performed. This analysis revealed that the overall flexibility and linearity of a given spectrin heterodimer and tetramer is largely determined by the intrinsic rigidity and linearity of its β-spectrin subunit. No additional rigidity appears to be imparted by noncovalent associations between the subunits. The scaled flexural rigidity of the most rigid spectrin analyzed (human brain) is similar to that reported for F-actin.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970120406
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Actin assembly and filament cross-linking in the presence of TW 260/240, the tissue-specific spectrin of the chicken intestinal brush border (1985)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 5 (1985), S. 311-322 
    Details
    ISSN: 0886-1544
    Keywords: Spectrin ; TW 260/240 ; chicken intestinal brush border ; actin assembly ; actin filament cross-linking ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: TW 260/240 is a tissue-specific spectrin found in the terminal web region of the chicken intestinal bruish border. We have examined the effects of TW 260/240 on assembly rates and critical concentrations (Co's) for monomer addition at the barbed and pointed ends of the actin filament. For these studies, acrosomal processes (AP) from Limulus sperm were used as nuclei for actin assembly. Under conditions which favor the interaction of TW 260/240 for actin (20-75 mM KCl, 2 mM Mg++) no effect on either elongation rates or Co's at either end of the actin filament was observed in the presence of this spectrinlike protein. The Limulus AP nucleation assay also allowed visualization of the kinetics of filament binding and cross-linking by TW 260/240. Ultrastructural analysis of TW 260/240 binding to actin filaments at their growing ends indicates that TW 260/240 tetramers bind laterally to the filament. Finally, evidence is presented that indicates that filaments cross-linked by TW 260/240 are stabilized against shear-dependent breakage.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970050404
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  • 3
    Electronic Resource
    Electronic Resource
    Isolation and characterization of sea urchin egg spectrin: Calcium modulation of the spectrin-actin interaction (1987)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 7 (1987), S. 304-314 
    Details
    ISSN: 0886-1544
    Keywords: spectrin-like ; actin-binding protein ; Ca++-regulated ; cytoskeleton ; eggs ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Sea urchin egg spectrin has been purified from a homogenate of unfertilized Strongylocentrotus purpuratus eggs using standard biochemical procedures. SDS-PAGE analysis of the molecule revealed a closely spaced, high molecular weight doublet at 237/234 kDa (present in an equimolar ratio). Rotary shadowed images of egg spectrin revealed a double-stranded, elongate, flexible rod-shaped contour, measuring 210 nm in length and ∼ 4-8 nm in width. Additionally, this molecule is shown to be immunologically related to avian erythroid spectrin, since it cross-reacts with antibodies prepared against the chicken erythrocyte α-spectrin/240 kDa subunit. The interaction of egg spectrin with actin was examined by sedimentation and falling-ball viscometry assays. The binding and cross linking properties of spectrin to actin demonstrate a unique Ca++-sensitive regulation at micromolar Ca++ concentrations. This observation provides new insight into the way Ca++ may regulate spectrin-actin interactions in vitro and further suggests possible structural and modulatory roles for egg spectrin in the developing sea urchin embryo.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970070403
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  • 4
    Electronic Resource
    Electronic Resource
    Functional diversity among spectrin isoforms (1989)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 12 (1989), S. 225-247 
    Details
    ISSN: 0886-1544
    Keywords: spectrin ; ankyrin ; protein 4.1 ; membrane skeleton ; spectrin-filament interaction ; fodrin ; adducin ; calpactin I ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The purpose of this review on spectrin is to examine the functional properties of this ubiquitous family of membrane skeletal proteins. Major topics include spectrin-membrane linkages, spectrin-filament linkages, the subcellular localization of spectrins in various cell types and a discussion of major functional differences between erythroid and nonerythroid spectrins. This includes a summary of studies from our own laboratories on the functional and structural comparison of avian spectrin isoforms which are comprised of a common alpha subunit and a tissue-specific beta subunit. Consequently, the observed differences among these spectrins can be assigned to differences in the properties of the beta subunits.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970120405
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