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Chromosomal proteins extracted from calf thymus by 0.35 M NaCl were insoluble at the low salt concentration needed initially for ion-exchange chromatography. However, the addition of high-affinity carboxymethyl-dextran rendered the precipitated proteins soluble, permitting them to be fractionated by elution from DEAE-Sephacel. In this way, the separation of HMG-1 from HMG-2 was achieved, as well as a partial fractionation of the low mobility group proteins, under conditions that did not disturb the native conformation of the proteins.
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