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October 1, 1980Journal of Biological ChemistryOpen Access

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

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Authors

HYH L YinYonsei UniversityTSTP StosselBrigham and Women's Hospital

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Overview

Biochemical analysis reveals structural and calcium-binding properties of gelsolin in rabbit lung macrophages, indicating its primary role in regulating actin gelation.

Key Points

  • To purify gelsolin from rabbit lung macrophages and determine its physicochemical and calcium-binding characteristics.
  • Purification of gelsolin from rabbit lung macrophage extracts.
  • Determination of physical constants including molecular weight, Stokes radius, sedimentation coefficient, and isoelectric point.
  • Measurement of calcium-binding stoichiometry and affinity in the presence of 0.1 M KCl and 2 mM MgCl2.
  • Gelsolin is identified as a single polypeptide chain with an average molecular weight of 91,000, a Stokes radius of 44 Å, a sedimentation coefficient (s20,w) of 4.9 S, an isoelectric point of 6.1, and a frictional ratio of 1.43.
  • The protein accounts for the majority of Ca2+-dependent regulation of actin gel-sol transformation in macrophage extracts.
  • Gelsolin binds 2 mol of Ca2+ per mole of protein with high affinity (Ka = 1.09 × 10^6 M^-1) under physiological salt conditions.

Cite This Study

Yin et al. (1980) studied this question.

synapsesocial.com/papers/6a7162acac440176ef2a0ffbhttps://doi.org/10.1016/s0021-9258(19)70589-4
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  5. 5Ca2+ control of actin gelation. Interaction of gelsolin with actin filaments and regulation of actin gelation.1980 · 260 citations