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- W1028420199 abstract "Publisher Summary Actobindin from Acanthamoeba castellanii has a profound inhibitory effect on actin polymerization. It is a Mr 9700 monomer (originally incorrectly thought to be a homodimer) that can be isolated from ameba by conventional chromatography. This chapter describes the original purification method with some modifications. The method is identical to that developed for the purification of Acanthamoeba profiling. A cell extract is applied to an anion-exchange column through which actobindin and the two isoforms of profilin pass with little retardation; the eluate is applied to a hydroxyapatite column, and the actobindin and two profiling isoforms that elute in the unbound fraction are separated by gel filtration. Because actobindin is very sensitive to proteolysis, the extraction procedure should be completed as rapidly as possible and the homogenization should not be too extensive in order to minimize the release of proteolytic enzymes. The addition of NaCl to the extraction buffer was initially arbitrary, although there is now some evidence that the binding of purified actobindin to phospholipids may be inhibited by high ionic strength. As actobindin does not bind to F-actin, the high concentration of NaCI has the added advantage of removing a significant amount of contaminating actin and F-actin-binding proteins in the initial high-speed centrifugation." @default.
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- W1028420199 date "1991-01-01" @default.
- W1028420199 modified "2023-09-27" @default.
- W1028420199 title "[11] Purification of actobindin from Acanthamoeba castellanii" @default.
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- W1028420199 doi "https://doi.org/10.1016/0076-6879(91)96013-h" @default.
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