The "in vitro motility assay" and phalloidin-F-actin.
We have compared the osmotic properties of the hydrated, native actin filament and of hydrated phalloidin-F-actin. We have found that phalloidin-F-actin interacts much more strongly with water than native F-actin. It is therefore very likely that the interaction with myosin (that requires the expulsion of the protein solvation water) is more problematic for phalloidin-F-actin that for native F-actin. We conclude that phalloidin-F-actin is not a bona fide substitute for native F-actin in the "in vitro motility assay".
Cuneo
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P
Dipartimento di Biochimica e Biologia Molecolare, Università di Ferrara, Italy.
Trombetta
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G
Magri
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E
Grazi
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E
D000199:Actins / Q000737:chemistry* / Q000378:metabolism; D000818:Animals; D018482:Muscle, Skeletal / Q000378:metabolism; D009997:Osmotic Pressure; D010590:Phalloidine / Q000737:chemistry* / Q000378:metabolism; D011092:Polyethylene Glycols; D011485:Protein Binding; D011817:Rabbits; D012996:Solutions
D000199:Actins; D012996:Solutions; D010590:Phalloidine; D011092:Polyethylene Glycols