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Alloaffinity filtration: A general approach to the purification of dynein and dynein-like molecules
Abstract
Alloaffinity filtration simply and specifically separates certain axonemal dyneins and dynein arm components from crude mixtures on the basis of their ability to bind and decorate Tetrahymena axonemal microtubules on a filter in the absence of ATP and to detach and pass into the eluate when 0.5 mM ATP is added. The procedure, which may be performed repetitively, is successful in purifying a Tetrahymena dynein that has characteristics of 30 S dynein prepared by conventional methods, while other dyneins originally present in the mixture, e.g., 14 S Tetrahymena dynein, are not found in the ATP eluate. A relatively homogeneous population of dynein oligomers is obtained. Alloaffinity-purified 30 S Tetrahymena dynein consists of heavy-, intermediate-, and light-chain polypeptides that cosediment in a sucrose gradient in fixed molar ratios and that have structural features of in situ Tetrahymena arms. Dyneins from other species will bind to Tetrahymena microtubules and can be purified by this method. Alloaffinity-purified Chlamydomonas dynein is a set of polypeptides including the four heavy chains that characterize the outer arm.
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Microtubule affinity has also been employed in the purification of other proteins such as MAP1, tau, and dynein.
“Microtubule affinity has also been employed in the purification of other proteins such as MAP1, tau, and dynein (Vallee and Bloom, 1984; Cleveland et al., 1977; Nasr and Satir, 1985).”
From Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility (1985) · cites this paper as Nasr and Satir, 1985
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Research works printed but not linked: 18
- Gibbons, 1965, Science (Washington, D. C.), 149, 424, 10.1126/science.149.3682.424 · DOI
- Satir, 1968, J. Cell Biol, 39, 77, 10.1083/jcb.39.1.77 · DOI
- Luck, 1984, J. Cell Biol, 98, 789, 10.1083/jcb.98.3.789 · DOI
- Bell, 1979, J. Supramol. Struct, 11, 311, 10.1002/jss.400110305 · DOI · Paper page
- Takahashi, 1978, J. Biochem. (Tokyo), 84, 1339, 10.1093/oxfordjournals.jbchem.a132256 · DOI
- Satir, 1981, Cell Motil, 1, 303, 10.1002/cm.970010304 · DOI
- Gaskin, 1974, J. Mol. Biol, 89, 737, 10.1016/0022-2836(74)90048-5 · DOI
- Hartree, 1972, Anal. Biochem, 48, 422, 10.1016/0003-2697(72)90094-2 · DOI
- Pallini, 1983, J. Submicrosc. Cytol, 15, 229
- Pollard, 1973, J. Biol. Chem, 248, 4682, 10.1016/S0021-9258(19)43718-6 · DOI
- Martin, 1975, J. Cell Biol, 67, 587, 10.1083/jcb.67.3.587 · DOI
- Witman, 1972, J. Cell Biol, 54, 507, 10.1083/jcb.54.3.507 · DOI
- Gibbons, 1966, J. Biol. Chem, 241, 5590, 10.1016/S0021-9258(18)96385-4 · DOI
- Piperno, 1979, J. Biol. Chem, 254, 3084, 10.1016/S0021-9258(17)30185-0 · DOI
- Inoue, 1976, J. Biochem. (Tokyo), 80, 1359, 10.1093/oxfordjournals.jbchem.a131409 · DOI
- Porter, 1983, J. Biol. Chem, 258, 6575, 10.1016/S0021-9258(18)32451-7 · DOI · Paper page
- Johnson, 1983, J. Cell Biol, 96, 669, 10.1083/jcb.96.3.669 · DOI · Paper page
- Witman, 1983, J. Submicrosc. Cytol, 15, 193
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Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility
VALE, R., REESE, T., & SHEETZ, M. (1985) · Cell · doi:10.1016/s0092-8674(85)80099-4 · Cited by 1,993
Metadata
- Authors
- Nasr, A., & Satir, P.
- Affiliations
- Albert Einstein College of Medicine (US)
- ORCID
- Satir, Peter
- Venue
- Analytical Biochemistry
- Publisher
- Elsevier BV
- Published
- 1985-11
- Volume
- 151
- Issue
- 1
- Pages
- 97-108
- ISSN
- 0003-2697 (ISSN-L)
- OpenAlex
- W2061061371
- Cited by
- 16
- References
- 0
- FWCI
- 1.76
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Analytical Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Heart, Lung, and Blood Institute (HL22560)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetic and Kidney Cyst Diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Keywords
- axonemal dynein, Tetrahymena, Chlamydomonas, dynein arms, microtubule binding, dynein heavy chain
- MeSH terms
- Adenosine Triphosphatases, Adenosine Triphosphate, Animals, Centrifugation, Density Gradient, Chlamydomonas, Cilia, Dyneins, Filtration, Microscopy, Electron, Microtubules, Molecular Weight, Protein Conformation, Tetrahymena
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