Differences between HMG1 proteins isolated from normal and tumour cells.
The properties of the non-histone chromosomal high-mobility-group 1 (HMG1) proteins from rat liver and Guerin ascites tumour cells (GAT cells) were compared and showed the following differences: (1) five spots were missing in the peptide map of HMG1 from GAT cells in comparison with that of HMG1 from rat liver; (2) HMG1 from GAT cells was about 5-times more poly(ADP)-ribosylated; (3) HMG1 from GAT cells which was found acetylated in vivo and incorporated [14C]acetate in vitro, whereas no incorporation of the label was detected in HMG1 from rat liver; (4) HMG1 from GAT cells exhibited pronounced ability to form oligomers at physiological ionic strength, while HMG1 from rat liver was predominantly in monomeric form. This property of HMG1 from GAT cells was lost upon deacetylation.
D000107:Acetylation; D000818:Animals; D002460:Cell Line; D004591:Electrophoresis, Polyacrylamide Gel; D006609:High Mobility Group Proteins / Q000378:metabolism*; D008099:Liver / Q000032:analysis*; D046911:Macromolecular Substances; D009374:Neoplasms, Experimental / Q000032:analysis*; D010446:Peptide Fragments; D011064:Poly Adenosine Diphosphate Ribose / Q000378:metabolism; D051381:Rats; D014357:Trypsin
D006609:High Mobility Group Proteins; D046911:Macromolecular Substances; D010446:Peptide Fragments; D011064:Poly Adenosine Diphosphate Ribose; D014357:Trypsin