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      Kinesin-related polypeptide is associated with vesicles from Corylus avellana pollen.

      Cell Motility and the Cytoskeleton
      Animals, Cattle, Centrifugation, Density Gradient, Chromatography, Gel, Electrophoresis, Polyacrylamide Gel, Golgi Apparatus, chemistry, metabolism, physiology, Immunohistochemistry, Kinesin, analysis, Microscopy, Immunoelectron, Microtubules, Molecular Weight, Organelles, Pollen, ultrastructure, Trees, Tubulin

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          Abstract

          A 100-kDa polypeptide with microtubule-interacting properties was identified in a Golgi vesicle-enriched fraction from Corylus avellana pollen. The k71s23 antibody (directed to the kinesin heavy chain from bovine brain) [Tiezzi et al., 1992: Cell Motil. Cytoskeleton 21:132-137] localized the polypeptide on the external surface of membrane-bounded organelles. Some 100-kDa-containing vesicles copelleted with microtubules (polymerized from purified bovine brain tubulin) either in presence or absence of 5 mM AMPPNP, but they could be released by 10 mM ATP or 0.5 M KCl. The pollen microtubule-interacting protein, salt-extracted from membranes and partially purified by gel filtration, exhibited an ATPase activity (16.2 nmolPi/mg/min) which could be stimulated about 2-fold (32.5 nmolPi/mg/min) by addition of bovine brain microtubules. We suppose that the 100-kDa polypeptide is part of a molecular complex showing properties of the kinesin class.

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