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) |
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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