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- W2057474512 abstract "The initial step in the purification of Dictyostelium myosin 11 heavy chain kinase A (MHCK A) is chromatography over phosphocellulose. Fractions containing MHCK A are pooled and chromatographed over a Mono Q column (Pharmacia LKB Biotechnology) equilibrated in 0.15 M KCl. Under these conditions MHCK A and most of the contaminating proteins elute in the flowthrough. The addition of Mg2+ and ATP to the Mono Q flowthrough results in the phosphorylation, within 15 min, of MHCK A to a level of 10 mol of phosphate per mole of 130-kDa kinase subunit. The hyperphosphorylated MHCK A binds to Mono Q columns in the presence of 0.15 M KCl and can be eluted, as a single homogeneous band, by a salt gradient to 0.35 m KCl. A similar purification procedure may prove useful for other proteins which can be highly phosphorylated. Hyperphosphorylation is shown to have no effect on the position at which MHCK A elutes from gel filtration columns (apparent Mr greater than 700,000)." @default.
- W2057474512 created "2016-06-24" @default.
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- W2057474512 date "1990-11-01" @default.
- W2057474512 modified "2023-09-26" @default.
- W2057474512 title "Purification of Dictyostelium myosin II heavy chain kinase a based on the increase in negative charge accompanying hyperphosphorylation" @default.
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- W2057474512 doi "https://doi.org/10.1016/1046-5928(90)90010-v" @default.
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