Saxton WM et al. (1988), Drosophila kinesin: characterization of microtu...

ECB-ART-32244

Proc Natl Acad Sci U S A 1988 Feb 01;854:1109-13. doi: 10.1073/pnas.85.4.1109.

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Drosophila kinesin: characterization of microtubule motility and ATPase.

Saxton WM , Porter ME , Cohn SA , Scholey JM , Raff EC , McIntosh JR .

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Preparations of kinesin, a microtubule-based force-producing protein, have been isolated from Drosophila melanogaster embryos by incubation of microtubules with a nonhydrolyzable ATP analogue and gel filtration of proteins released from the microtubules by ATP. These preparations induced MgATP-dependent microtubule gliding in vitro with a Km for MgATP of 44 microM and a Vmax for gliding of 0.9 micron/sec. Samples of Drosophila proteins that were active in motility assays possessed an average ATPase activity in solution of 17 nmol/min per mg that increased to an average of 106 nmol/min per mg in the presence of microtubules. The major polypeptides that copurified with these activities showed relative molecular masses of 115 kDa and 58 kDa. An antiserum raised against the 115-kDa polypeptide also recognized the 110-kDa component of squid kinesin preparations and the 130-kDa component of sea urchin kinesin preparations.

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Genes referenced: LOC100887844 LOC581395

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