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The crude cytoplasmic extracts of macrophages showed a low actin-polymerization activity as compared with the purified actin preparations. This suggested that an actin-polymerization inhibitor should exist in the crude cytoplasmic extracts of macrophages. Thus, the isolation of actin-polymerization inhibiting protein from the crude extract was attempted. The protein with a high actin-polymerization inhibiting activity had a molecular weight of 65,000 daltons as determined by polyacrylamide gel electrophoresis in dodecyl sulfate, a Stokes radius of 33.8 A as measured by gel filtration and a sedimentation coefficient of 4.9 S as determined by analytical centrifugation. The actin-polymerization inhibiting activity was much higher in 0.1 M KCl than in 0.6 M KCl. It was not affected by either the presence or the absence of free Ca2+. It was considered that the protein is responsible for the large proportion of unpolymerized actin in the crude extract of macrophages.

Protein from macrophages inhibiting polymerization of actin.