Abstract
Proteins extracted from chicken erythrocyte chromatin with 0.35 m NaCl are analyzed by two-dimensional gel electrophoresis. The well-defined high mobility group (HMG) proteins are identified on the electrophoretogram. All but one of the HMG proteins as well as a number of other nonhistone proteins in the extract are sufficiently basic that they are observed only if the first dimension is carried out as nonequilibrium pH gradient electrophoresis. Protein fractions obtained by precipitation at several trichloroacetic acid concentrations are examined by two-dimensional gel electrophoresis and the term “HMG protein” discussed in light of the results.
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