Purification and phosphorylation of initiation factor eIF-2 from rabbit skeletal muscle |
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Authors: | Christopher G. Proud Virginia M. Pain |
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Affiliation: | School of Biological Sciences, University of Sussex, Falmer, Brighton, BN1 9QG, England |
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Abstract: | Core particle DNA unfolding and refolding are followed by stopped-flow circular dichroism technique. When core particles are dissociated in the stopped-flow cuvette, the high CD deviation corresponding to the dissociated state is reached in the first millisecond, which means that the dissociation process is completed within the dead time of the apparatus which is ~1 ms. The same conclusion can be drawn when core particles are reassociated, since the low CD value, typical of the associated state, is immediately reached. Similarly histone release from chromatin is a very fast process. We also include some points of discussion about core particle assembly process. |
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Keywords: | Skeletal muscle Initiation factor-2 Protein phosphorylation Tris Tris(hydroxymethyl)aminomethane EDTA ethylenediamine tetraacetic acid EGTA HCR haem-controlled repressor eIF-2 eucaryotic initiation factor-2 eIF-2α eIF-2β, α,β subunits of eIF-2 SDS sodium dodecylsulphate |
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