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- W2016770179 abstract "Using the binding of heterologous, rhodamine phalloidin-labelled F-actinin vitro, two F-actin binding proteins were identified in protein extracts from the green algaChara corallinaafter fractionation by anion exchange chromatography. The first protein, a putative myosin, released laterally bound F-actin at ATP-concentrations as low as 1μm; equivalent concentrations of ADP were not effective. Binding of F-actin was inhibited by the sulfhydryl-alkylating agent N-ethylmaleimide (NEM). Binding of F-actin was also abolished by a monoclonal anti-myosin (J14) previously used for immunodetection and immunolocalization in internodal cells (Groliget al., 1988,Eur J Cell Biol47: 22–31). Immunoblotting with J14 detected a 110kDa polypeptide only in those protein fractions that had revealed ATP-sensitive binding of F-actin. The putative myosin bound with mediocre affinity to immobilized calmodulin and free Ca2+-concentration made no difference to this binding affinity. In contrast to the putative myosin, the second, less abundant protein revealed ATP-insensitive and end-wise binding to the microfilament and was not recognized by the anti-myosin antibody." @default.
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- W2016770179 date "1996-05-01" @default.
- W2016770179 modified "2023-09-24" @default.
- W2016770179 title "PARTIAL CHARACTERIZATION OF A PUTATIVE 110kDa MYOSIN FROM THE GREEN ALGACHARA CORALLINABYIN VITROBINDING OF FLUORESCENT F-ACTIN" @default.
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- W2016770179 doi "https://doi.org/10.1006/cbir.1996.0043" @default.
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