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- W1522015108 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." @default.
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- W1522015108 date "1980-10-01" @default.
- W1522015108 modified "2023-10-18" @default.
- W1522015108 title "Purification and structural properties of gelsolin, a Ca2+-activated regulatory protein of macrophages." @default.
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- W1522015108 doi "https://doi.org/10.1016/s0021-9258(19)70589-4" @default.
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