Abstract
We describe the purification procedure and some of the physiochemical properties of gelsolin, a major Ca2+-dependent regulatory protein of actin gel-sol transformation in rabbit lung macrophages. Gelsolin accounts for the majority of Ca2+ control of actin gelation in macrophage extracts. It is a single polypeptide chain with an average molecular weight of 91,000 a Stokes radius of 44 A, a sedimentation coefficient (s20(0),w) of 4.9 S, an isoelectric point of 6.1, and a frictional ratio of 1.43. Gelsolin binds 2 mol of Ca2+ with high affinity (Ka 1.09 X 10(6) M-1) in the presence of 0.1 M KCl and 2 mM MgCl2.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 9490-9493 |
| Number of pages | 4 |
| Journal | Journal of Biological Chemistry |
| Volume | 255 |
| Issue number | 19 |
| State | Published - Oct 10 1980 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology