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Actin in the Ciliated Protozoan Climacostomum Virens: Purification by DNAse I Affinity Chromatography, Electrophoretic Characterization, and Immunological Analysis

Actin in the Ciliated Protozoan Climacostomum Virens: Purification by DNAse I Affinity Chromatography, Electrophoretic Characterization, and Immunological Analysis

J F Fahrni

Cell Motil Cytoskeleton. 1992;22(1):62-71.

PMID: 1581980

Abstract:

The anti-actin monoclonal antibody (mab) JLA20 (Lin: Proc. Natl. Acad. Sci. U.S.A. 78:2335-2339, 1981) labels a 43 kD protein on Western blots of Climacostomum cell extracts; this protein does not react with an anti-alpha-smooth muscle actin mab (Skalli et al.: J. Cell Biol. 103:2787-2796, 1986) nor with an anti-alpha-sarcomeric actin mab (Skalli et al.: Am. J. Pathol. 130:515-531, 1988). This protein binds to DNAse I and can be purified by DNAse I affinity chromatography. The affinity-purified actin also reacts with mab JLA20. Two-dimensional gel analysis reveals that Climacostomum actin focuses as three spots which are more basic than the mammalian actin isoforms. After addition of KCl, the affinity-purified actin polymerizes into filaments as shown by electron microscopy after negative staining.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42413882	Monoclonal Anti-Actin, α-Smooth Muscle			Price

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