Abstract:
:Measurement of the binding equilibrium for the interaction of alpha-actinin with F-actin is complicated by secondary reactions involving cross-linking and/or bundling of the actin filaments. To quantitate the initial binding event, we studied the interaction of the bacterially expressed actin-binding domain (ABD) of chick smooth muscle alpha-actinin with F-actin. Stopped-flow measurements revealed a quench in protein fluorescence and an enhancement in light scattering when ABD binds to F-actin yielding second order rate constants for association of 2 x 10(5), 1.8 x 10(6) and 4 x 10(6) M-1.s-1 at 5 degrees C, 15 degrees C and 25 degrees C, respectively. At the latter two temperatures the dissociation rate constants were 1.5 and 9.6s-1, giving equilibrium constants of 0.83 and 2.4 microM, respectively. Optical changes on mixing intact alpha-actinin with F-actin were dominated by secondary bundling events.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Kuhlman PA,Ellis J,Critchley DR,Bagshaw CRdoi
10.1016/0014-5793(94)80434-6subject
Has Abstractpub_date
1994-02-21 00:00:00pages
297-301issue
3eissn
0014-5793issn
1873-3468pii
0014-5793(94)80434-6journal_volume
339pub_type
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