The Journal of Cell Biology, Vol 94, 51-55, Copyright © 1982 by The Rockefeller University Press
Effect of actin-binding protein on the sedimentation properties of actin
S Rosenberg and A Stracher
Actin and actin-binding protein (ABP) have recently been purified from
human platelet cytoskeletons (S. Rosenberg, A. Stracher, and R.C. Lucas,
1981, J. Cell Biol. 91:201-211). Here, the effect of ABP on the
sedimentation of actin was studied. When ABP was added to preformed F-
actin filaments, it bound until a maximum ratio of 1:9 (ABP:actin, mol:mol)
was reached. however, when actin was polymerized in the presence of ABP,
two and a half times more ABP was able to bind to the actin- that is, every
3.4 actin monomers were now bound by an ABP dimer. ABP was not able to
induce the sedimentation of actin under nonpolymerizing conditions but was
able to reduce the time and concentration of actin required for
sedimentation under slow polymerizing conditions. ABP, therefore, exerts
its effect of G-actin by either nucleating polymerization or by
cross-linking newly formed oligomers into a more sedimentable form.
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