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Mabuchi, I. (1983) An actin-depolymerixing protein (depactin) from starfish oocytes: Properties and interaction with actin. J.Cell Biol. 97, 1612-1621
Physico-chemical properties and interaction with actin of an actin-depolymerizing protein from mature starfish oocyte were studied. This protein, which is called depactin, exists in a monomeric form under physiological conditions.  Its molecular weight is ~20,000 for the native protein and ~17,000 for denatured protein.  The Glu + Asp/Lys + Arg molar ratio of this protein is 1.55.  The apparent pI of the denatured depactin is ~6.
The extent of actin polymerization is reduced by the presence of depactin; however, the rate of polymerization seems to be accelerated as measured spectrophotometrically at 238nm. This effect is interpreted to indicate that depactin cut the newly formed filaments into small fragments, thereby increasing the number of the filament ends onto which monomers are added.  The apparent critical concentration of actin for polymerization, as determined by viscometry or flow birefringence measurement, is increased by the presence of depactin in a concentration-dependent manner.  Raising the pH of the solution does not reverse the action of depactin.  The molar ratio of actin and depactin, which interact with each other, is estimated to be 1:1 by means of a cross-linking experiment using a water-soluble carbodiimide. Depactin binds to a DNase I-sepharose column via actin and is selectively eluted with 0.6M KCl or 0.6M KI. The association constant between actin and depactin is estimated, using the column, to be 2-3x106M-1.
The constant of depactin in the high-speed supernatant of the oocyte extract is determined to be 1%; this can act upon ~63% of the actin in the supernatant.
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