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  • Articles: DFG German National Licenses  (3)
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  • Articles: DFG German National Licenses  (3)
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  • 1
    Electronic Resource
    Electronic Resource
    COMPARATIVE STUDIES ON THE CHARACTERISTIC PROPERTIES OF TWO FORMS OF BRAIN ACTIN SEPARABLE BY ISOELECTRIC FOCUSSING (1979)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 32 (1979), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— Actin isolated from 10-day embryonic chick brain produced a single band indistinguishable from that of muscle actin when electrophoresed in sodium dodecyl sulfate-polyacrylamide gel. Isoelectric focussing in polyacrylamide gel showed that the isolated protein was composed of two components–the β and γ forms of actin previously detected in other mammalian nonmuscle cells and tissues–in a molar ratio of 1.1/1.0. The same ratio was observed in a sonicate of 10-day embryonic chick brain and in various actin-containing fractions at each step of an actin purification procedure which involved gel filtration chromatography and polymerization-depolymerization of the protein. Additionally, the two forms of actin were found to co-precipitate with muscle myosin and to bind to a DNase I-agarose affinity column in this ratio. In contrast, a third isoelectrically distinct protein with the same electrophoretic mobility as actin was found in the whole brain sonicate, but not in any of the actin-containing fractions examined. When cellular protein in neuronal and non-neuronal cell populations isolated from 10-day embryonic chick brain was analyzed, it was found that β and β actins were also present in each class of cells in the molar ratio of 1.1/1.0. However, this ratio decreased slightly during development of the chick brain. We conclude from this study that the β and γ forms of brain actin are very similar in several characteristic properties of actin, and that it is unlikely that brain cells utilize different forms of the protein for different types of cell motility.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1979.tb04591.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Cytochalasin D inhibits actin polymerization and induces depolymerization of actin filaments formed during platelet shape change (1981)
    [s.l.] : Nature Publishing Group
    Nature 293 (1981), S. 302-305 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Fig. 1 a, Dose-response curve for cytochalasin inhibition of actin poly-merization in thrombin-stimulated platelets. o Indicates preincubation of platelet samples with the designated concentration of cytochalasin D (CD) ( + 1% DMSO) for 60s before stimulation with thrombin. Controls are indicated ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/293302a0
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Complexes containing actin and spectrin from erythrocyte and brain (1983)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 3 (1983), S. 375-382 
    Details
    ISSN: 0886-1544
    Keywords: actin ; spectrin ; band 4.1 ; cytochalasins ; erythrocyte ; brain ; actin-membrane attachment ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A complex of proteins with properties similar to those of erythrocyte spectrinband 4.1-actin complex has been idientified in a preparation derived from bovine brain. The complex has an apparent sedimentation coefficient of about 26S, and contains brain spectrin (also called fodrin) and actin as major components. The actin in the complex is in the oligomeric form, which nucleates assembly of actin filaments that grow from the “barbed” end. The complex cross-links actin filaments, resulting in an increase in low-shear viscosity. Whether the complex contains a protein analogous to erythrocyte band 4.1 is not known. However, it can be demonstrated that brain spectrin has the capability to interact with band 4.1 in a way which increases its ability to cross-link actin filaments.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970030505
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    Paper (German National Licenses)
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