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Evidence that the 116 kDa component of kinesin binds and hydrolyses ATP
Author(s) -
Penningroth Stephen M.,
Rose Patricia M.,
Peterson Dolores D.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80220-x
Subject(s) - kinesin , microtubule , atpase , protein subunit , motility , chemistry , adenosine triphosphate , microbiology and biotechnology , biochemistry , biophysics , enzyme , biology , gene
Kinesin was prepared from bovine brain as described previously for studies of translocation. A major component of kinesin, (116 kDa) was shown to undergo specific photocrosslinking with [α‐ 32 P]ATP, indicating it was an ATP‐binding polypeptide. A low ATPase activity associated with kinesin was stimulated up to 5‐fold by microtubules to a specific activity of 14 nmol·min −1 ·mg −1 . N ‐Ethylmaleimide inhibited both [α‐ 32 P]ATP binding to the 116 kDa polypeptide and microtubule‐stimulated ATPase activity, suggesting that the 116 kDa polypeptide was the catalytic subunit of kinesin. Though the ATPase activity associated with kinesin is low, it may be sufficient to support motility assuming it is coupled to the velocity of translocation.