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J Biol Chem ; 276(30): 28014-21, 2001 Jul 27.
Article in English | MEDLINE | ID: mdl-11382767

ABSTRACT

We have developed a strategy for the purification of native microtubule motor proteins from mitotic HeLa cells and describe here the purification and characterization of human conventional kinesin and two human kinesin-related proteins, HSET and CENP-E. We found that the 120-kDa HeLa cell conventional kinesin is an active motor that induces microtubule gliding at approximately 30 microm/min at room temperature. This active form of HeLa cell kinesin does not contain light chains, although light chains were detected in other fractions. HSET, a member of the C-terminal kinesin subfamily, was also purified in native form for the first time, and the protein migrates as a single band at approximately 75 kDa. The purified HSET is an active motor that induces microtubule gliding at a rate of approximately 5 microm/min, and microtubules glide for an average of 3 microm before ceasing movement. Finally, we purified native CENP-E, a kinesin-related protein that has been implicated in chromosome congression during mitosis, and we found that this form of CENP-E does not induce microtubule gliding but is able to bind to microtubules.


Subject(s)
Chromosomal Proteins, Non-Histone/chemistry , Kinesins/chemistry , Centrifugation, Density Gradient , Chromatography, Gel , Chromosomal Proteins, Non-Histone/isolation & purification , Electrophoresis, Polyacrylamide Gel , HeLa Cells , Humans , Kinesins/isolation & purification , Microtubules/chemistry , Mitosis , Protein Binding , Protein Structure, Tertiary
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