Abstract
A method for the efficient and practical large-scale purification of high-mobility group (HMG) non-histone chromosomal proteins, HMG1 and HMG2, from porcine thymus applying Polybuffer-exchanger PBE94 gel as anion-exchanger has been developed. This method affords higher resolution, purity and yield, than the conventional procedure of CM-Sephadex C-25 ion-exchange column chromatography. Furthermore, use of Polybuffer-exchanger PBE94 column chromatography led to direct preparation of HMG1 and HMG2 from loosely bound non-histone chromosomal protein fraction of chromatin without prefractional precipitation with trichloroacetic acid or prior extraction with perchloric acid. Thus, the application of PBE94 gel as an anion-exchanger to the subfractionation of other kinds of homologous protein is possible.
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