Purification and structural properties of gelsolin, a Ca2+-activated regulatory protein of macrophages.

H. L. Yin, T. P. Stossel

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122 Scopus citations


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 languageEnglish (US)
Pages (from-to)9490-9493
Number of pages4
JournalJournal of Biological Chemistry
Issue number19
StatePublished - Oct 10 1980


ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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