title: The interaction of nonhistone chromosomal proteins HMG1 and HMG2 with subfractions of H1 histone immobilized on agarose.
abstract: Chromatographically isolated subfractions of calf thymus H1 histone have been covalently coupled to agarose beads and tested for their ability to form complexes with the non-histone proteins HMG1 and HMG2 (High Mobility Group proteins, Walker, J.M., Goodwin, G.H. and Johns, E.W. (1976) Eur. J. Biochem. 62, 461-469). When a mixture of HMG1 and HMG2 is passed through a column of H1 histone-agarose, the HMG2 does not bind. HMG1 does bind and can be eluted from the column with NaCl in the range of 0.05 M--0.15 M. The NaCl concentration required to elute HMG1 from each of the three H1 histone subfraction coulmns is different, suggesting that HMG1 has a different binding affinity for the three H1 histone subfractions.
mesh_terms: D000818:Animals; D002417:Cattle; D002846:Chromatography, Affinity; D002868:Chromosomal Proteins, Non-Histone / Q000302:isolation & purification; D004591:Electrophoresis, Polyacrylamide Gel; D006657:Histones; D011485:Protein Binding; D012685:Sepharose; D013950:Thymus Gland
chemical_list: D002868:Chromosomal Proteins, Non-Histone; D006657:Histones; D012685:Sepharose