Bovine brain kinesin is a microtubule-activated ATPase
Open accessAbstract
Recently, a protein called kinesin was described, which is capable of inducing movement of inert particles along microtubules. To purify this protein from bovine brain, we used the ability of kinesin to bind to taxol-stabilized microtubules in the presence of inorganic tripolyphosphate. The brain kinesin preparation contained one major polypeptide of 135 kDa and four minor polypeptides of 45-70 kDa. The minor polypeptides were eluted from a gel-permeation chromatography column at the same position as the major component. All the polypeptides of the preparation were capable of binding to the microtubules under identical conditions. The kinesin molecule is most probably a complex of these polypeptides. Brain kinesin had a very low ATPase activity (0.06-0.08 mumol X min-1 X mg-1 in 3 mM Mg2+ at pH 6.7). ATPase activity was strongly stimulated by microtubules (Vmax = 4.6 mumol per min per mg of kinesin). Microtubule-activated kinesin ATPase had a Km for ATP between 10 and 12 X 10(-6) M and a Kapp for microtubules (i.e., polymerized tubulin concentration required for a half-maximal activation) of 12-14 X 10(-6) M. Kinesin had a significant ATPase activity even without microtubules if 2 mM Ca2+ was substituted for Mg2+ (Vmax = 1.6 mumol X min-1 X mg-1; Km = 800 X 10(-6) M). Kinesin is therefore a mechanochemical ATPase that is activated by microtubules.
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Kinesin is commonly purified at pH 6.6-6.8, whereas the lysates in this study were analyzed at pH 7.2-7.4.
“since kinesin is commonly purified at pH 6.6–6.8 (Kuznetsov and Gelfand, 1986; Hackney, 1988; Wagner et al., 1989, 1991), whereas our lysates were analyzed at pH 7.2–7.4.”
From Light Chain– dependent Regulation of Kinesin's Interaction with Microtubules (1998) · cites this paper as Kuznetsov and Gelfand, 1986
Purification of kinesin is performed at the nonphysiological pH of 6.6-6.8.
“Purification of kinesin is performed at the nonphysiological pH of 6.6–6.8 (Kuznetsov and Gelfand, 1986; Wagner et al., 1989, 1991; Hackney, 1991).”
From Light Chain– dependent Regulation of Kinesin's Interaction with Microtubules (1998) · cites this paper as Kuznetsov and Gelfand, 1986
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- Authors
- Kuznetsov, S. A., & Gelfand, V. I.
- Affiliations
- Lomonosov Moscow State University (RU)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1986-11
- Volume
- 83
- Issue
- 22
- Pages
- 8530-8534
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC386964
- OpenAlex
- W2007253244
- Cited by
- 217
- References
- 17
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 1 · 2023: 1 · 2022: 3 · 2021: 1 · 2020: 1 · 2018: 1 · 2017: 2 · 2016: 3 · 2012: 3
- FWCI
- 10.17
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Health Sciences › Medicine › Oncology › Cancer Treatment and Pharmacology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetic and Kidney Cyst Diseases
- Keywords
- kinesin, bovine brain, microtubule binding, taxol-stabilized microtubules, ATPase activity
- MeSH terms
- Adenosine Triphosphatases, Adenosine Triphosphate, Adenylyl Imidodiphosphate, Animals, Brain Chemistry, Cattle, Enzyme Activation, Hydrolysis, Kinetics, Microtubule Proteins, Microtubules, Nerve Tissue Proteins, Polyphosphates, Kinesins
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