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- W1520641343 abstract "Publisher Summary This chapter discusses the purification of actin and actin-associated proteins from yeast and presents updated methods for isolating yeast actin and actin-associated proteins that may facilitate the biochemical analyses of the yeast actin cytoskeleton. It also presents a detailed outline of the DNase I affinity method for purifying yeast actin. This method is based on the reconstitution of actin assembly in soluble yeast extracts and allows a one-step isolation of a semi-intact actin cytoskeleton. Some of the most common uses for purified yeast actin are (1) testing the ability of a protein to cosediment with filamentous actin, (2) testing the effects of an actin-binding protein on actin assembly and/or actin disassembly kinetics, (3) determining the structures and/or activities of mutant actins. Using additional chromatography steps, various components can be isolated, providing the opportunity to study the activities of native actin-associated proteins from wild-type and mutant strains." @default.
- W1520641343 created "2016-06-24" @default.
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- W1520641343 date "2002-01-01" @default.
- W1520641343 modified "2023-10-10" @default.
- W1520641343 title "Purification of yeast actin and actin-associated proteins" @default.
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- W1520641343 doi "https://doi.org/10.1016/s0076-6879(02)51862-0" @default.
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