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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 22 (1992), S. 245-249 
    ISSN: 0886-1544
    Keywords: rhodamine phalloidin ; anti-chicken actin antibody ; plant actin ; DNase I ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Previous reports about phalloidin binding to plant actins have been indirect. We present here evidence showing that phalloidin does bind and stabilize filaments of actin extracted from pea roots. Criteria for the presence of actin included stabilization as a polymer in the presence of phalloidin, cross-reaction with antibody against chicken actin, affinity binding to DNase I, and ability to be decorated by the S1 fragment of rabbit muscle myosin.Phalloidin was able to stabilize polymers in pea root extracts against dissociation during SDS gel electrophoresis, and these polymers were shown to be composed exclusively of actin. Pea root actin isolated by affinity chromatography on a DNase I column was incubated with rhodamine phalloidin and electrophoresed on a native gel. The rhodamine fluorescence remained with the stabilized filaments, indicating clearly that phalloidin does bind to actin from a plant source. © 1992 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 29 (1994), S. 339-344 
    ISSN: 0886-1544
    Keywords: microfilament ; phalloidin ; immunoblotting ; immunocytochemistry ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Anti-actin monoclonal antibodies were prepared using phalloidin-stabilized actin that was purified from pea roots by DNase I affinity chromatography. One monoclonal antibody, designated mAb3H11, bound plant actin in preliminary screenings and was further analyzed. Immunoblot analysis showed that this antibody had a high affinity for plant actin in crude and purified preparations but a low affinity for rabbit muscle actin. In immunoblots of plant extracts separated on two-dimensional gels it appeared to bind all actin isoforms recognized by the JLA20 anti-chicken actin antibody. Using immunofluorescent cytochemistry, the antibody was used to observe actin filaments in aldehyde-fixed and methanol-treated tobacco protoplasts. These results indicate that mAb3H11 should be a useful reagent for the study of plant actins. © 1994 Wiley-Liss, Inc.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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