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  • Title: Purification of a low molecular weight non-histone chromosomal protein.
    Author: Montagna RA, Becker FF.
    Journal: Biochim Biophys Acta; 1980; 606(1):148-56. PubMed ID: 7353013.
    Abstract:
    A non-histone chromosomal proteins was extracted from rat liver chromatin with 0.35 M NaCl and purified more than 2758 times to near homogeneity by hydroxyapatite, gel filtration, and phosphocellulose chromatography. The final fraction was greater than 95% pure as judged by non-denaturing gel electrophoresis. The protein, designated loosely bound non-histone chromosomal protein 1, had an observed molecular weight of 15 700. This protein was demonstrated to increase the amount of RNA synthesized in a heterologous (Escherichia coli RNA polymerase) transcription system and, therefore, this activity was also used to monitor its purification. The availability of highly purified loosely bound non-histone chromosomal protein 1 will make possible an examination of its structural and/or functional role in chromatin.
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