Submolecular domains of bovine brain kinesin identified by electron microscopy and monoclonal antibody decoration

@article{Hirokawa1989SubmolecularDO,
  title={Submolecular domains of bovine brain kinesin identified by electron microscopy and monoclonal antibody decoration},
  author={Nobutaka Hirokawa and Katherine Pfister and Hiroshi Yorifuji and Mark C. Wagner and Scott T. Brady and George S. Bloom},
  journal={Cell},
  year={1989},
  volume={56},
  pages={867-878}
}

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Identification of globular mechanochemical heads of kinesin

The results show that the two heavy chains of native kinesin are arranged in parallel, and that the 45K fragments, which display nucleotide-sensitive interactions with microtubules12,13, represent mechanochemical 'heads' located at the N-terminal regions of the heavy chains.

Monoclonal antibodies to kinesin heavy and light chains stain vesicle- like structures, but not microtubules, in cultured cells

Results constitute the first direct evidence for the association of kinesin with membrane-bounded organelles, and suggest a molecular mechanism for organelle motility based on transient interactions of organelle-bound kinesIn with microtubule surface, in double-labeling experiments using antibodies to kines in and tubulin, kinesine-containing particles were most abundant in regions where microtubules were most highly concentrated.

The molecular structure of adrenal medulla kinesin.

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Kinesin, a protein that transports particles along microtubules, has been purified from pig brain, following published methods and appears to be a rod with a large branched structure at one end and a small fork at the other.

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